P59237 (ALR2_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine racemase, catabolic
EC=5.1.1.1

Gene names

Name:	dadX
Ordered Locus Names:	c1639

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA By similarity. HAMAP MF_01201
Catalytic activity	L-alanine = D-alanine. HAMAP MF_01201
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01201
Pathway	Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP MF_01201
Sequence similarities	Belongs to the alanine racemase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alanine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	alanine racemase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Alanine racemase, catabolic HAMAP MF_01201		PRO_0000114518
Sites
	Active site	35	1	Proton acceptor; specific for D-alanine By similarity
	Active site	253	1	Proton acceptor; specific for L-alanine By similarity
Amino acid modifications
	Modified residue	35	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	26 – 27	2	PY → TH in AAC61705. Ref.1
	Sequence conflict	50	1	L → I in AAC61705. Ref.1
	Sequence conflict	171 – 172	2	SA → GR in AAC61705. Ref.1
	Sequence conflict	190	1	A → S in AAC61705. Ref.1
	Sequence conflict	199	1	Q → P in AAC61705. Ref.1
	Sequence conflict	215	1	A → R in AAC61705. Ref.1
	Sequence conflict	281	1	P → L in AAC61705. Ref.1
	Sequence conflict	292	1	L → R in AAC61705. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P59237 [UniParc]. Last modified January 27, 2003. Version 1. Checksum: 4DF10C5843374659	FASTA	356	38,869
	10 20 30 40 50 60 MTRPIQASLD LQALKQNLSI VRQAAPYARV WSVVKANAYG HGIERIWSAL GATDGFALLN 70 80 90 100 110 120 LEEAITLRER GWKGPILMLE GFFHAQDLEI YDQHRLTTCV HSNWQLKALQ NARLKAPLDI 130 140 150 160 170 180 YLKVNSGMNR LGFQPDRVLT VWQQLRAMAN VGEMTLMSHF AEAEHPDGIS SAMARIEQAA 190 200 210 220 230 240 EGLECRRSLA NSAATLWHQE AHFDWVRPGI ILYGASPSGQ WRDIANTGLR PVMTLSSEII 250 260 270 280 290 300 GVQTLKAGER VGYGGRYTAR DEQRIGIVAA GYADGYPRHA PTGTPVLVDG VLTMTVGTVS 310 320 330 340 350 MDMLAVDLTP CPQAGIGTPV ELWGKEIKID DVAAAAGTVG YELMCALALR VPVVTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic analysis of a pathogenicity island in uropathogenic Escherichia coli CFT073: distribution of homologous sequences among isolates from patients with pyelonephritis, cystitis, and catheter-associated bacteriuria and from fecal samples." Guyer D.M., Kao J.-S., Mobley H.L.T. Infect. Immun. 66:4411-4417(1998) [PubMed: 9712795] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.
[2]	"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF081283 Genomic DNA. Translation: AAC61705.1. AE014075 Genomic DNA. Translation: AAN80104.1.
RefSeq	NP_753544.1. NC_004431.1.
3D structure databases
ProteinModelPortal	P59237.
SMR	P59237. Positions 3-356.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000041767; EBESCP00000040116; EBESCG00000040817.
GeneID	1035411.
GenomeReviews	Gene locus c1639 in contig AE014075_GR.
KEGG	ecc:c1639.
NMPDR	fig|199310.1.peg.1587.
PATRIC	18281206. VBIEscCol75197_1524.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009862.
HOGENOM	HBG712172.
OMA	NWQIKAL.
PhylomeDB	P59237.
ProtClustDB	PRK03646.
Family and domain databases
HAMAP	MF_01201. Ala_racemase. [Tree]
InterPro	IPR000821. Ala_racemase. IPR009006. Ala_racemase/Decarboxylase_C. IPR011079. Ala_racemase_C. IPR001608. Ala_racemase_N. IPR020622. Ala_racemase_pyridoxalP-BS. [Graphical view]
Gene3D	G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit.
KO	K01775.
Pfam	PF00842. Ala_racemase_C. 1 hit. PF01168. Ala_racemase_N. 1 hit. [Graphical view]
PRINTS	PR00992. ALARACEMASE.
SMART	SM01005. Ala_racemase_C. 1 hit. [Graphical view]
SUPFAM	SSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMs	TIGR00492. Alr. 1 hit.
PROSITE	PS00395. ALANINE_RACEMASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALR2_ECOL6

Accession

Primary (citable) accession number: P59237

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program