Caulobacter crescentus CB15 Protein Class: a protein complex

Superclasses: a complex
a protein

An instance of this class defines a multimeric protein complex consisting of multiple aggregated polypeptide chains. It may be chemically modified. It may be a homomultimer or a heteromultimer. Its components may themselves be protein complexes.

Child Classes: a 3-methyl-2-oxobutanoate dehydrogenase (0), a branched-chain 2-keto acid dehydrogenase (0), a citrate lyase (0), a complement 5b (0), a cysteine desulfurylase (0), a DsrC sulfur carrier protein (0), a DsrEFH complex (0), a factor X (0), a factor Xa (0), a factor XI (0), a factor XIa (0), a glutamine synthetase (0), a hemoglobin (0), a holo-[carbon monoxide dehydrogenase] (0), a holo-[methylmalonyl-CoA:pyruvate carboxytransferase] (0), a hydrogenase (0), a hydrogenase 3 (0), a lactyl-CoA dehydratase (0), a NifDK protein complex (0), a NifDK protein containing an M-cluster (0), a NifEN protein complex (0), a NifEN protein complex containing an L-cluster (0), a NifEN protein complex containing an M-cluster (0), a nitrate reductase (0), a nitrogenase complex (0), a phosphatase-2A (0), a phosphorylase a (0), a phosphorylase b (0), a phosphorylated isocitrate dehydrogenase (0), a plasmin (0), a procollagen (0), a pyruvate dehydrogenase (0), a pyruvate formate-lyase (0), a pyruvate,water dikinase (0), a reduced electron-transferring flavoprotein (0), a ribonucleoside triphosphate reductase (0), a Ribulose Bisphosphate Carboxylase/Oxygenase (0), a SoxZY protein (0), a thyroglobulin (0), a xanthine dehydrogenase (0), a xanthine oxidase (0), a [chaperone-ADP]-[disordered-form scaffold protein] complex (0), a [chaperone-ATP]-[co-chaperone]-[scaffold protein-(2Fe-2S)] complex (0), a [co-chaperone]-[scaffold protein-(2Fe-2S)] complex (0), a [cysteine desulfurase]-(S-sulfanyl)2-[disordered-form scaffold protein] complex (0), a [cysteine desulfurase]-S-sulfanyl-[disordered-form scaffold protein] complex (0), a [cysteine desulfurase]-[scaffold protein-(2Fe-2S)] complex (0), a [glycogenin] (0), a [holo-acyl-carrier-protein] synthase (0), an acetyl-CoA carboxylase (0), an acetyl-[holo citrate lyase acyl-carrier protein] (0), an apo-[carbon monoxide dehydrogenase] (0), an apo-[methylmalonyl-CoA:pyruvate carboxytransferase] (0), an isocitrate dehydrogenase (0), an RNA polymerase (0), an S-sulfanyl-[cysteine desulfurase]-S-sulfanyl-[disordered-form scaffold protein] complex (0), an S-sulfanyl-[cysteine desulfurase]-[disordered-form scaffold protein] complex (0), an [acetyl-CoA carboxylase] phosphate (0), citramalate lyase, active (0), citramalate lyase, inactive (0), Ent-B (0), Flavorubredoxin (0), Nr-I (0), Nr-II (0), Tap-Un (0), Tar-Un (0), Trg-Un (0), Tsr-Un (0), [a holo citrate lyase acyl-carrier protein] (0), [a holo malonate decarboxylase acyl-carrier-protein] (0), [a pyruvate, water dikinase]-phosphate (0), [a SoxY protein] (0), [a SoxZY protein]-thiocysteine-sulfate (0), [an apo citrate-lyase acyl-carrier protein] (0), [an apo malonate decarboxylase acyl-carrier protein] (0), [DsrEFH complex] persulfide (0)

2-oxoglutarate dehydrogenase,
5-methyltetrahydrofolate--homocysteine methyltransferase,
acetolactate synthase,
acetyl-CoA carboxylase,
acetyl-CoA carboxylase,
alkyl hydroperoxide reductase,
ATP synthase F0,
ATP synthase F1,
ATP synthase F1F0,
biotin carboxyl carrier protein (dimer),
carbamoyl-phosphate synthase,
cysteine synthase,
cytochrome c oxidase,
cytochrome c oxidase,
cytochrome d ubiquinol oxidase,
cytochrome d ubiquinol oxidase,
DNA gyrase,
DNA polymerase III,
DNA polymerase III,
DNA-directed RNA polymerase,
glutamate synthase,
glutamyl-tRNA(Gln) amidotransferase,
glycine cleavage system P protein,
glycyl-tRNA synthetase,
isopropylmalate dehydratase,
isopropylmalate dehydratase,
isoquinoline 1-oxidoreductase,
isoquinoline 1-oxidoreductase,
methylmalonyl-CoA mutase,
methylmalonyl-CoA mutase,
NAD(P) transhydrogenase,
NADH dehydrogenase I,
NADH dehydrogenase I,
nitrite reductase [NAD(P)H],
oxoadipate CoA-transferase,
oxoadipate CoA-transferase,
phenylalanyl-tRNA synthetase,
phosphoribosylaminoimidazole carboxylase,
phosphoribosylformylglycinamidine synthase,
potassium-transporting ATPase,
predicted ATP transporter of a sugar,
predicted ATP transporter of cystine,
predicted ATP transporter of Fe,
predicted ATP transporter of Mo2+,
predicted ATP transporter of NO3-,
predicted ATP transporter of phosphate,
predicted ATP transporter of phosphonate,
predicted ATP transporter of SO42-,
predicted export of protoheme,
predicted transporter of putrescine,
propionyl-CoA carboxylase,
protocatechuate 3,4-dioxygenase,
pyruvate dehydrogenase complex,
pyruvate dehydrogenase complex, E1 component,
riboflavin synthase,
ribonucleoside-diphosphate reductase,
ribonucleoside-diphosphate reductase,
ribonucleoside-diphosphate reductase,
ribosomal pseudouridine synthase,
succinate dehydrogenase,
succinate dehydrogenase,
succinyl-CoA synthetase,
sulfate adenylate transferase,
sulfite reductase (NADPH) flavoprotein,
topoisomerase IV,
tRNA pseudouridine synthase,
tryptophan synthase,
ubiquinol oxidase,
ubiquinol oxidase,
ubiquinol-cytochrome c reductase,
vanillate O-demethylase,
xanthine dehydrogenase,
xanthine dehydrogenase


Bagchi05: Bagchi A, Ghosh TC (2005). "A structural study towards the understanding of the interactions of SoxY, SoxZ, and SoxB, leading to the oxidation of sulfur anions via the novel global sulfur oxidizing (sox) operon." Biochem Biophys Res Commun 335(2);609-15. PMID: 16084835

Cort08: Cort JR, Selan U, Schulte A, Grimm F, Kennedy MA, Dahl C (2008). "Allochromatium vinosum DsrC: solution-state NMR structure, redox properties, and interaction with DsrEFH, a protein essential for purple sulfur bacterial sulfur oxidation." J Mol Biol 382(3);692-707. PMID: 18656485

Dahl08: Dahl C, Schulte A, Stockdreher Y, Hong C, Grimm F, Sander J, Kim R, Kim SH, Shin DH (2008). "Structural and molecular genetic insight into a widespread sulfur oxidation pathway." J Mol Biol 384(5);1287-300. PMID: 18952098

Dahl13: Dahl C, Franz B, Hensen D, Kesselheim A, Zigann R (2013). "Sulfite oxidation in the purple sulfur bacterium Allochromatium vinosum: identification of SoeABC as a major player and relevance of SoxYZ in the process." Microbiology 159(Pt 12);2626-38. PMID: 24030319

Eisenberg00: Eisenberg D, Gill HS, Pfluegl GM, Rotstein SH (2000). "Structure-function relationships of glutamine synthetases." Biochim Biophys Acta 1477(1-2);122-45. PMID: 10708854

Elovson68: Elovson J, Vagelos PR (1968). "Acyl carrier protein. X. Acyl carrier protein synthetase." J Biol Chem 1968;243(13);3603-11. PMID: 4872726

Friedrich00: Friedrich CG, Quentmeier A, Bardischewsky F, Rother D, Kraft R, Kostka S, Prinz H (2000). "Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17." J Bacteriol 182(17);4677-87. PMID: 10940005

Grein10: Grein F, Pereira IA, Dahl C (2010). "Biochemical Characterization of Individual Components of the Allochromatium vinosum DsrMKJOP Transmembrane Complex Aids Understanding of Complex Function In Vivo." J Bacteriol 192(24);6369-77. PMID: 20952577

Hedderich04: Hedderich R (2004). "Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I." J Bioenerg Biomembr 36(1);65-75. PMID: 15168611

Hu06: Hu Y, Corbett MC, Fay AW, Webber JA, Hodgson KO, Hedman B, Ribbe MW (2006). "FeMo cofactor maturation on NifEN." Proc Natl Acad Sci U S A 103(46);17119-24. PMID: 17050696

Hunt75: Hunt JB, Smyrniotis PZ, Ginsburg A, Stadtman ER (1975). "Metal ion requirement by glutamine synthetase of Escherichia coli in catalysis of gamma-glutamyl transfer." Arch Biochem Biophys 166(1);102-24. PMID: 235885

Kaiser11: Kaiser JT, Hu Y, Wiig JA, Rees DC, Ribbe MW (2011). "Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase." Science 331(6013);91-4. PMID: 21212358

Liaw94: Liaw SH, Eisenberg D (1994). "Structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes." Biochemistry 33(3);675-81. PMID: 7904828

Liaw95: Liaw SH, Kuo I, Eisenberg D (1995). "Discovery of the ammonium substrate site on glutamine synthetase, a third cation binding site." Protein Sci 4(11);2358-65. PMID: 8563633

Lin91: Lin EC, Iuchi S (1991). "Regulation of gene expression in fermentative and respiratory systems in Escherichia coli and related bacteria." Annu Rev Genet 1991;25;361-87. PMID: 1812811

Markley13: Markley JL, Kim JH, Dai Z, Bothe JR, Cai K, Frederick RO, Tonelli M (2013). "Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery." FEBS Lett. PMID: 23333622

Nilekani83: Nilekani S, SivaRaman C (1983). "Purification and properties of citrate lyase from Escherichia coli." Biochemistry 1983;22(20);4657-63. PMID: 6354265

OrmeJohnson92: Orme-Johnson WH (1992). "Nitrogenase structure: where to now?." Science 257(5077);1639-40. PMID: 1529351

Polacco81: Polacco ML, Cronan JE (1981). "A mutant of Escherichia coli conditionally defective in the synthesis of holo-[acyl carrier protein]." J Biol Chem 1981;256(11);5750-4. PMID: 7016860

Quentmeier01: Quentmeier A, Friedrich CG (2001). "The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17." FEBS Lett 503(2-3);168-72. PMID: 11513876

Quentmeier03: Quentmeier A, Hellwig P, Bardischewsky F, Grelle G, Kraft R, Friedrich CG (2003). "Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein." Biochem Biophys Res Commun 312(4);1011-8. PMID: 14651972

Richards94: Richards AJ, Lowe DJ, Richards RL, Thomson AJ, Smith BE (1994). "Electron-paramagnetic-resonance and magnetic-circular-dichroism studies of the binding of cyanide and thiols to the thiols to the iron-molybdenum cofactor from Klebsiella pneumoniae nitrogenase." Biochem J 297 ( Pt 2);373-8. PMID: 8297344

Schedel79: Schedel, M., Vanselow, M., Trueper, H. G. (1979). "Siroheme sulfite reductase from Chromatium vinosum. Purification and investigation of some of its molecular and catalytic properties." Arch. Microbiol. 121: 29-36.

Silberg01: Silberg JJ, Hoff KG, Tapley TL, Vickery LE (2001). "The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli." J Biol Chem 276(3);1696-700. PMID: 11053447

Silberg04: Silberg JJ, Tapley TL, Hoff KG, Vickery LE (2004). "Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU." J Biol Chem 279(52);53924-31. PMID: 15485839

Sun10: Sun J, Hopkins RC, Jenney FE, McTernan PM, Adams MW (2010). "Heterologous expression and maturation of an NADP-dependent [NiFe]-hydrogenase: a key enzyme in biofuel production." PLoS One 5(5);e10526. PMID: 20463892

Venceslau14: Venceslau SS, Stockdreher Y, Dahl C, Pereira IA (2014). "The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism." Biochim Biophys Acta 1837(7);1148-64. PMID: 24662917

Vignais08: Vignais PM (2008). "Hydrogenases and H(+)-reduction in primary energy conservation." Results Probl Cell Differ 45;223-52. PMID: 18500479

Wiig11: Wiig JA, Hu Y, Ribbe MW (2011). "NifEN-B complex of Azotobacter vinelandii is fully functional in nitrogenase FeMo cofactor assembly." Proc Natl Acad Sci U S A 108(21);8623-7. PMID: 21551100

Wiseman08: Wiseman JM, Ifa DR, Zhu Y, Kissinger CB, Manicke NE, Kissinger PT, Cooks RG (2008). "Desorption electrospray ionization mass spectrometry: Imaging drugs and metabolites in tissues." Proc Natl Acad Sci U S A 105(47);18120-5. PMID: 18697929

Yamashita89: Yamashita MM, Almassy RJ, Janson CA, Cascio D, Eisenberg D (1989). "Refined atomic model of glutamine synthetase at 3.5 A resolution." J Biol Chem 264(30);17681-90. PMID: 2572586

Zheng97: Zheng L, White RH, Dean DR (1997). "Purification of the Azotobacter vinelandii nifV-encoded homocitrate synthase." J Bacteriol 179(18);5963-6. PMID: 9294461

Zhou03b: Zhou J, Pham HT, Ruediger R, Walter G (2003). "Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution." Biochem J 369(Pt 2);387-98. PMID: 12370081

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