Q65YW7 (Q65YW7_STRLA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Alanine racemase HAMAP MF_01201 RuleBase RU000608
EC=5.1.1.1 HAMAP MF_01201 RuleBase RU000608

Gene names

Name:

alr HAMAP MF_01201 EMBL BAD44772.1

Organism

Streptomyces lavendulae subsp. lavendulae EMBL BAD44772.1

Taxonomic identifier

58340 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Provides the D-alanine required for cell wall biosynthesis By similarity. HAMAP MF_01201
Catalytic activity	L-alanine = D-alanine. HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006
Pathway	Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP MF_01201 SAAS SAAS009006 RuleBase RU004247 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_01201
Sequence similarities	Belongs to the alanine racemase family. HAMAP MF_01201 RuleBase RU004188

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation HAMAP MF_01201 Peptidoglycan synthesis HAMAP MF_01201
Ligand	Pyridoxal phosphate HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006 PDB 1VFH
Molecular function	Isomerase SAAS SAAS009006 HAMAP MF_01201 RuleBase RU000608
Technical term	3D-structure PDB 1VFH PDB 1VFS PDB 1VFT
Gene Ontology (GO)
Biological process	alanine metabolic process Inferred from electronic annotation. Source: HAMAP cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
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
Sites
	Active site	38	1	Proton acceptor; specific for D-alanine By similarity HAMAP MF_01201
	Active site	270	1	Proton acceptor; specific for L-alanine By similarity HAMAP MF_01201
Amino acid modifications
	Modified residue	38	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01201
	Modified residue	38	1	Pyridoxal phosphate PDB 1VFH
	Modified residue	129	1	N6-carboxylysine PDB 1VFH PDB 1VFS PDB 1VFT

Sequences

	Sequence		Length	Mass (Da)
	Q65YW7 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 292ADA9BFF81D75D	FASTA	378	39,890
	10 20 30 40 50 60 MNETPTRVYA EIDLDAVRAN VRALRARAPR SALMAVVKSN AYGHGAVPCA RAAQEAGAAW 70 80 90 100 110 120 LGTATPEEAL ELRAAGIQGR IMCWLWTPGG PWREAIETDI DVSVSGMWAL DEVRAAARAA 130 140 150 160 170 180 GRTARIQLKA DTGLGRNGCQ PADWAELVGA AVAAQAEGTV QVTGVWSHFA CADEPGHPSI 190 200 210 220 230 240 RLQLDAFRDM LAYAEKEGVD PEVRHIANSP ATLTLPETHF DLVRTGLAVY GVSPSPELGT 250 260 270 280 290 300 PAQLGLRPAM TLRASLALVK TVPAGHGVSY GHHYVTESET HLALVPAGYA DGIPRNASGR 310 320 330 340 350 360 GPVLVAGKIR RAAGRIAMDQ FVVDLGEDLA EAGDEAVILG DAERGEPTAE DWAQAAHTIA 370 YEIVTRIGGR VPRVYLGG

References

[1]

"Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine." Noda M., Kawahara Y., Ichikawa A., Matoba Y., Matsuo H., Lee D.G., Kumagai T., Sugiyama M. J. Biol. Chem. 279:46143-46152(2004) [PubMed: 15302885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.

[2]

"Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product." Noda M., Matoba Y., Kumagai T., Sugiyama M. J. Biol. Chem. 279:46153-46161(2004) [PubMed: 15302886] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), CARBOXYLATION AT LYS-129, PYRIDOXAL PHOSPHATE AT LYS-38.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB176676 Genomic DNA. Translation: BAD44772.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VFH	X-ray	2.00	A	1-378	[»]
1VFS	X-ray	1.90	A/B	1-378	[»]
1VFT	X-ray	2.30	A/B	1-378	[»]

ProteinModelPortal

Q65YW7.

SMR

Q65YW7. Positions 3-378.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

5.1.1.1. 190739.

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.

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

Q65YW7_STRLA

Accession

Primary (citable) accession number: Q65YW7

Entry history

Integrated into UniProtKB/TrEMBL:	October 25, 2004
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)