Reviewed, UniProtKB/Swiss-Prot P06191 (ALR2_SALTY)

Names and origin

Protein names

Recommended name:
    Alanine racemase, catabolic
    EC=5.1.1.1

Gene names

Name:	dadX
Synonyms:	dadB
Ordered Locus Names:	STM1802

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

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

General annotation (Comments)

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

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome Direct protein sequencing
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_0000114561
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 HAMAP MF_01201

Sequences

	Sequence		Length	Mass (Da)
	P06191-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 43DF23205EF25C69	FASTA	356	38,804
	10 20 30 40 50 60 MTRPIQASLD LQVMKQNLAI VRRAAPEARV WSVVKANAYG HGIERVWSAL GATDGFAMLN 70 80 90 100 110 120 LEEAITLRER GWKGPILMLE GFFHAQDLEA YDTYRLTTCI HSNWQLKALQ NARLNAPLDI 130 140 150 160 170 180 YVKVNSGMNR LGFQPERAQT VWQQLRAMRN VGEMTLMSHF AQADHPEGIG EAMRRIALAT 190 200 210 220 230 240 EGLQCAYSLS NSAATLWHPQ AHYDWVRPGI ILYGASPSGQ WRDIADTGLK PVMTLSSEII 250 260 270 280 290 300 GVQTLSAGER VGYGGGYSVT QEQRIGIVAA GYADGYPRHA PTGTPVLVDG IRTRTVGTVS 310 320 330 340 350 MDMLAVDLTP CPQAGIGTPV ELWGKEIKVD DVASAAGTLG YELLCAVAPR VPFVTT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catabolic alanine racemase from Salmonella typhimurium: DNA sequence, enzyme purification, and characterization." Wasserman S.A., Daub E., Grisafi P., Botstein D., Walsh C.T. Biochemistry 23:5182-5187(1984) [PubMed: 6391537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 1-25.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of beta-substituted alanines: kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism." Badet B., Roise D., Walsh C.T. Biochemistry 23:5188-5194(1984) [PubMed: 6439236] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-44.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K02119 Genomic DNA. Translation: AAA27054.1. AE006468 Genomic DNA. Translation: AAL20717.1.
PIR	A29519.
RefSeq	NP_460758.1.
3D structure databases
SMR	P06191. Positions 3-354.
ModBase	Search...
Proteomic databases
PRIDE	P06191.
Genome annotation databases
GeneID	1253321.
GenomeReviews	Gene locus STM1802 in contig AE006468_GR.
KEGG	stm:STM1802.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG712172.
OMA	FFHADEL.
Enzyme and pathway databases
BioCyc	STYP99287:STM1802-MONOMER.
BRENDA	5.1.1.1. 2.
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_SALTY

Accession

Primary (citable) accession number: P06191

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	February 9, 2010
This is version 82 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)