A9IU63 (ALR_BORPD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine racemase
EC=5.1.1.1

Gene names

Name:	alr
Ordered Locus Names:	Bpet3162

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella petrii

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity.
Catalytic activity	L-alanine = D-alanine. HAMAP-Rule MF_01201
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule 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	D-alanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
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 – 376	376	Alanine racemase HAMAP-Rule MF_01201		PRO_1000138582
Sites
	Active site	44	1	Proton acceptor; specific for D-alanine By similarity
	Active site	271	1	Proton acceptor; specific for L-alanine By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	319	1	Substrate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	44	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9IU63 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 548CEC69C2969A7E	FASTA	376	39,291
	10 20 30 40 50 60 MPRPIHASIS LAALAHNLDV VRRHLDQAAQ AAGGAPPSIW AVIKANAYGH GIEAAVAGFS 70 80 90 100 110 120 AAQGLAMLDL AEAVRCREAG WGGPILLLEG FFQPADLDLI DRYHLSATVH TREQLDMLAQ 130 140 150 160 170 180 ARLSRRVDIM LKLNSGMNRL GFDPDAYGSA HARALQLREQ GVVGAVGRMT HFACADGTPG 190 200 210 220 230 240 VAGQLRVFQS VTQGLADGPV SVCNSAATLR YPEIAVAHGA QAHWVRPGIC LYGASPFADA 250 260 270 280 290 300 DAASFGLRPA MSLRSQIIGV QDLPAGAEVG YGATFRAERP MRVGVVACGY ADGYPRHAGT 310 320 330 340 350 360 GTPVVVGGVR TRLVGRVSMD MLMVDLDPVP AAGIGTPVSL WGQDGPSVDE VAQAAGTIGY 370 ELLCALAPRV PVKRDS

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP43504.1.
RefSeq	YP_001631772.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9IU63.
ModBase	Search...
Protein-protein interaction databases
STRING	340100.Bpet3162.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAP43504; CAP43504; Bpet3162.
GeneID	5820170.
KEGG	bpt:Bpet3162.
PATRIC	21167883. VBIBorPet31633_3187.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0787.
HOGENOM	HOG000031446.
KO	K01775.
OMA	GQWQDIA.
ProtClustDB	CLSK920285.
Enzyme and pathway databases
BioCyc	BPET340100:GJBO-3204-MONOMER.
UniPathway	UPA00042; UER00497.
Family and domain databases
Gene3D	2.40.37.10. 1 hit.
HAMAP	MF_01201. Ala_racemase.
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.
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

ALR_BORPD

Accession

Primary (citable) accession number: A9IU63

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program