Q837J0 (Q837J0_ENTFA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Alanine racemase HAMAP-Rule MF_01201
EC=5.1.1.1 HAMAP-Rule MF_01201

Gene names

Name:	alr EMBL AAO80661.1
Ordered Locus Names:	EF_0849 EMBL AAO80661.1

Organism

Enterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP] EMBL AAO80661.1

Taxonomic identifier

226185 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Enterococcaceae › Enterococcus › Enterococcus faecalis

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. HAMAP-Rule MF_01201
Catalytic activity	L-alanine = D-alanine. HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622
Pathway	Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201 RuleBase RU004247 SAAS SAAS020622
Sequence similarities	Belongs to the alanine racemase family. HAMAP-Rule MF_01201 RuleBase RU004188

Ontologies

Keywords
Ligand	Pyridoxal phosphate HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622
Molecular function	Isomerase SAAS SAAS020622 HAMAP-Rule MF_01201 RuleBase RU000608
Technical term	3D-structure PDB 3E5P PDB 3E6E Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-alanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	alanine racemase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	40	1	Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
	Active site	267	1	Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
	Binding site	139	1	Substrate By similarity HAMAP-Rule MF_01201
	Binding site	314	1	Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201
Amino acid modifications
	Modified residue	40	1	N6-(pyridoxal phosphate)lysine PDB 3E5P
	Modified residue	40	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

	Sequence		Length	Mass (Da)
	Q837J0 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4DE356FE62478E0B	FASTA	371	40,980
	10 20 30 40 50 60 MVVGWHRPTR LHIDTQAITE NVQKECQRLP EGTALFAVVK ANGYGHGAVE SAKAAKKGGA 70 80 90 100 110 120 TGFCVALLDE AIELREAGVQ DPILILSVVD LAYVPLLIQY DLSVTVATQE WLEAALQQLT 130 140 150 160 170 180 PESNTPLRVH LKVDTGMGRI GFLTPEETKQ AVRFVQSHKE FLWEGIFTHF STADEIDTSY 190 200 210 220 230 240 FEKQAGRFKA VLAVLEELPR YVHVSNSATA LWHPDVPGNM IRYGVAMYGL NPSGNKLAPS 250 260 270 280 290 300 YALKPALRLT SELIHVKRLA AGEGIGYGET YVTEAEEWIG TVPIGYADGW LRHLQGFTVL 310 320 330 340 350 360 VNGKRCEIVG RVCMDQCMIR LAEEVPVGSV VTLVGKDGNE ENTLQMVAEK LETIHYEVAC 370 TFSQRIPREY N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M. Science 299:2071-2074(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700802 / V583.
[2]	"Structural insights into the alanine racemase from Enterococcus faecalis." Priyadarshi A., Lee E.H., Sung M.W., Nam K.H., Lee W.H., Kim E.E., Hwang K.Y. Biochim. Biophys. Acta 1794:1030-1040(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016830 Genomic DNA. Translation: AAO80661.1.

RefSeq

NP_814591.1. NC_004668.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E5P	X-ray	2.50	A/B/C	1-371	[»]
3E6E	X-ray	2.50	A/B/C	1-371	[»]

ProteinModelPortal

Q837J0.

ModBase

Search...

Protein-protein interaction databases

STRING

226185.EF0849.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAO80661; AAO80661; EF_0849.

GeneID

1199742.

KEGG

efa:EF0849.

PATRIC

21852074. VBIEntFae7065_0786.

Phylogenomic databases

KO

K01775.

OMA

CENDSEV.

Enzyme and pathway databases

BioCyc

EFAE226185:GHI1-830-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...

Other

EvolutionaryTrace

Q837J0.

Entry information

Entry name

Q837J0_ENTFA

Accession

Primary (citable) accession number: Q837J0

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	May 29, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)