twitter

MetaCyc Enzyme: altronate oxidoreductase

Gene: uxaB Accession Numbers: EG11065 (MetaCyc), b1521, ECK1514

Species: Escherichia coli K-12 substr. MG1655

Summary:
Altronate oxidoreductase is the second enzyme of the galacturonate catabolism pathway, catalyzing the reversible NADH-dependent reduction of D-tagaturonate to D-altronate [Portalier72].

The reaction proceeds via an ordered bi-bi mechanism with NADH as the first substrate [Portalier72a].

Locations: cytosol

Map Position: [1,607,253 <- 1,608,704]

Molecular Weight of Polypeptide: 54.808 kD (from nucleotide sequence)

pI: 5.25

Unification Links: ASAP:ABE-0005076 , CGSC:16 , EchoBASE:EB1058 , EcoGene:EG11065 , EcoliWiki:b1521 , ModBase:P0A6L7 , OU-Microarray:b1521 , PortEco:uxaB , PR:PRO_000024204 , Pride:P0A6L7 , Protein Model Portal:P0A6L7 , RefSeq:YP_025302 , RegulonDB:EG11065 , SMR:P0A6L7 , String:511145.b1521 , UniProt:P0A6L7

Relationship Links: InterPro:IN-FAMILY:IPR008927 , InterPro:IN-FAMILY:IPR013118 , InterPro:IN-FAMILY:IPR013131 , InterPro:IN-FAMILY:IPR013328 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR023668 , Pfam:IN-FAMILY:PF01232 , Pfam:IN-FAMILY:PF08125

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0019698 - D-galacturonate catabolic process Inferred from experiment [Blanco83]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0009026 - tagaturonate reductase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Portalier72a]
GO:0051287 - NAD binding Inferred from experiment [Portalier72]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01]
GO:0050662 - coenzyme binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Enzymatic reaction of: altronate oxidoreductase

Synonyms: tagaturonate reductase, tagaturonate dehydrogenase, D-altronate:NAD+ 3-oxidoreductase

EC Number: 1.1.1.58

D-altronate + NAD+ <=> D-tagaturonate + NADH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible. [Hickman60]

Alternative Substrates for NADH: NADPH [Portalier82 ]

In Pathways: superpathway of hexuronide and hexuronate degradation , superpathway of microbial D-galacturonate and D-glucuronate degradation , D-galacturonate degradation I

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International

Summary:
The pH optimum for the NADH oxidation reaction is 8.9. NADPH can substitute for NADH at ~10% efficiency, but only in the direction of D-tagaturonate reduction [Portalier82].

Inhibitors (Competitive): D-fructuronate [Portalier72a, Comment 1] , D-mannonate [Portalier72a, Comment 2]

Inhibitors (Unknown Mechanism): p-chloromercuribenzoate [Hickman60, Portalier82, Comment 3]

Kinetic Parameters:

Substrate
Km (μM)
Citations
D-tagaturonate
100.0
[Hickman60, BRENDA14]
D-tagaturonate
350.0
[Portalier72, BRENDA14]
D-tagaturonate
670.0
[Portalier82, BRENDA14]
D-tagaturonate
670.0
[Portalier72a, BRENDA14]
NADH
60.0
[Portalier72, BRENDA14]
NADH
85.0
[Portalier82, BRENDA14]
NADH
85.0
[Portalier72a, BRENDA14]
D-altronate
90.0
[Portalier72b, BRENDA14]
D-altronate
75.0, 53.0
[Portalier82, BRENDA14]
D-altronate
75.0, 53.0
[Portalier72a, BRENDA14]
NAD+
88.0
[Portalier72b, BRENDA14]
NAD+
110.0
[Portalier72, BRENDA14]
NAD+
75.0, 53.0
[Portalier82, BRENDA14]
NAD+
75.0, 53.0
[Portalier72a, BRENDA14]

pH(opt): 6 [BRENDA14, Hickman60], 8.9 [BRENDA14, Portalier82], 6.3 [Portalier72]


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 18 -> 29
[UniProt10]
UniProt: NAD; Non-Experimental Qualifier: by similarity;

History:
10/20/97 Gene b1521 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11065.


References

Blanco83: Blanco C, Mata-Gilsinger M, Ritzenthaler P (1983). "Construction of hybrid plasmids containing the Escherichia coli uxaB gene: analysis of its regulation and direction of transcription." J Bacteriol 153(2);747-55. PMID: 6296052

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hickman60: Hickman J, Ashwell G (1960). "Uronic acid metabolism in bacteria. II. Purification and properties of D-altronic acid and D-mannonic acid dehydrogenases in Escherichia coli." J Biol Chem 235;1566-70. PMID: 14401695

Portalier72: Portalier RC, Stoeber FR (1972). "[D-altronate: NAD-oxidoreductase in Escherichia coli K12. Purification, properties, and specificity]." Eur J Biochem 1972;26(1);50-61. PMID: 4402917

Portalier72a: Portalier RC (1972). "[D-altronate: NAD-oxidoreductase from Escherichia coli K12. Kinetic studies]." Eur J Biochem 1972;30(2);211-9. PMID: 4351434

Portalier72b: Portalier RC, Stoeber FR (1972). "[Colorimetric determinations of aldonate oxidoreductases of Escherichia coli K 12: applications]." Biochim Biophys Acta 289(1);19-27. PMID: 4564054

Portalier82: Portalier R, Stoeber F (1982). "D-Mannonate and D-altronate-NAD dehydrogenases from Escherichia coli." Methods Enzymol 89 Pt D;210-8. PMID: 6755169

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Mon Mar 30, 2015, biocyc12.