Reviewed, UniProtKB/Swiss-Prot Q8X4I9 (ALR2_ECO57)

Names and origin

Protein names

Recommended name:
    Alanine racemase, catabolic
    EC=5.1.1.1

Gene names

Name:	dadX
Synonyms:	dadB
Ordered Locus Names:	Z1953, ECs1685

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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
Induction	By alanine. HAMAP MF_01201
Sequence similarities	Belongs to the alanine racemase family.
Sequence caution	The sequence BAB35108.1 differs from that shown. Reason: Frameshift at position 321.

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: HAMAP peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	alanine racemase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding 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 – 356	356	Alanine racemase, catabolic HAMAP MF_01201		PRO_0000114519
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	314 – 315	2	AG → RD in BAB35108. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8X4I9-1 [UniParc]. Last modified March 5, 2002. Version 1. Checksum: 28B67F19517A3B09	FASTA	356	38,859
	10 20 30 40 50 60 MTRPIQASLD LQALKQNLSI VRQAAPHARV WSVVKANAYG HGIERIWSAL GATDGFALLN 70 80 90 100 110 120 LEEAITLRER GWKGPILMLE GFFHAQDLEM YDQHRLTTCV HSNWQLKALQ NARLKAPLDI 130 140 150 160 170 180 YLKVNSGMNR LGFQPDRVLT VWQQLRAMAN VGEMTLMSHF AEAEHPDGIS GAMARIEQAA 190 200 210 220 230 240 EGLECRRSLS NSAATLWHPE AHFDWVRPGI ILYGASPSGQ WRDIANTGLR PVMTLSSEII 250 260 270 280 290 300 GVQTLKAGER VGYGGRYTAR DEQRIGIVAA GYADGYPRHA PTGTPVLVDG VRTMTVGTVS 310 320 330 340 350 MDMLAVDLTP CPQAGIGTPV ELWGKEIKID DVAAAAGTVG YELMCALALR VPVVTV

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56041.1. BA000007 Genomic DNA. Translation: BAB35108.1. Frameshift.
PIR	E85697. E90839.
RefSeq	NP_287429.1. NP_309712.1.
3D structure databases
SMR	Q8X4I9. Positions 3-354.
ModBase	Search...
Genome annotation databases
GeneID	913184. 960219.
GenomeReviews	Gene locus Z1953 in contig AE005174_GR. Gene locus ECs1685 in contig BA000007_GR.
KEGG	ece:Z1953. ecs:ECs1685.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG712172.
OMA	FFHADEL.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS1685-MONOMER.
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]
Pfam	PF00842. Ala_racemase_C. 1 hit. PF01168. Ala_racemase_N. 1 hit. [Graphical view]
PRINTS	PR00992. ALARACEMASE.
TIGRFAMs	TIGR00492. alr. 1 hit.
PROSITE	PS00395. ALANINE_RACEMASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALR2_ECO57

Accession

Primary (citable) accession number: Q8X4I9
Secondary accession number(s): Q8X2W4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 5, 2002
Last modified:	February 9, 2010
This is version 61 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)