Reviewed, UniProtKB/Swiss-Prot Q0THR7 (UXAB_ECOL5)

Names and origin

Protein names

Recommended name:
    Altronate oxidoreductase
    EC=1.1.1.58
Alternative name(s):
    Tagaturonate reductase
    Tagaturonate dehydrogenase

Gene names

Name:	uxaB
Ordered Locus Names:	ECP_1505

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	D-altronate + NAD(+) = D-tagaturonate + NADH.
Pathway	Carbohydrate metabolism; pentose and glucuronate interconversion.
Sequence similarities	Belongs to the mannitol dehydrogenase family. UxaB subfamily.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro tagaturonate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 483	483	Altronate oxidoreductase		PRO_1000044703
Regions
	Nucleotide binding	18 – 29	12	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0THR7-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 19A2AD0049367426	FASTA	483	54,860
	10 20 30 40 50 60 MKTLNRRDFP GAQYPERIIQ FGEGNFLRAF VDWQIDLLNE HTDLNSGVVV VRPIETSFPP 70 80 90 100 110 120 SLSTQDGLYT TIIRGLNEKG EAVSDARLIR SVNREISVYS EYDEFLKLAH NPEMRFVFSN 130 140 150 160 170 180 TTEAGISYHA GDKFDDAPAV SYPAKLTRLL FERFSHFNGA LDKGWIIIPC ELIDYNGDAL 190 200 210 220 230 240 RELVLRYAQE WALPEAFIQW LDQANSFCST LVDRIVTGYP RDEVAKLEEE LGYHDGFLDT 250 260 270 280 290 300 AEYFYLFVIQ GPKSLATELR LDKYPLNVLI VDDIKPYKER KVAILNGAHT ALVPVAFQAG 310 320 330 340 350 360 LDTVGEAMND AEICAFVEKA IYEEIIPVLD LPRDELESFA SAVTGRFRNP YIKHQLLSIA 370 380 390 400 410 420 LNGMTKFRTR ILPQLLAGQK ANGTLPARLT FALAALIAFY RGERNGETYP VQDDAHWLER 430 440 450 460 470 480 YQQLWSQYRD RVIGTQELVA IVLAEKDHWE QDLTQVPGLV EQVANDLDAI LEKGMREAVR PLC

References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000247 Genomic DNA. Translation: ABG69512.1.
RefSeq	YP_669413.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4187930.
GenomeReviews	Gene locus ECP_1505 in contig CP000247_GR.
KEGG	ecp:ECP_1505.
NMPDR	fig|340197.3.peg.4284.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0THR7.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_1505-MON.
Family and domain databases
HAMAP	MF_00670. [Tree]
InterPro	IPR013328. DHase_multihelical. IPR013118. Mannitol_DHase_C. IPR013131. Mannitol_DHase_N. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
Pfam	PF01232. Mannitol_dh. 1 hit. PF08125. Mannitol_dh_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UXAB_ECOL5

Accession

Primary (citable) accession number: Q0THR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	November 25, 2008
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)