Reviewed, UniProtKB/Swiss-Prot Q9RER4 (ALR_AQUPY)

Names and origin

Protein names

Recommended name:
    Alanine racemase
    EC=5.1.1.1

Gene names

Name:

alr

Organism

Aquifex pyrophilus

Taxonomic identifier

2714 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Provides the D-alanine required for cell wall biosynthesis. 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 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_01201
Miscellaneous	Strong thermostability. HAMAP MF_01201
Sequence similarities	Belongs to the alanine racemase family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
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
Molecule processing
	Chain	1 – 341	341	Alanine racemase HAMAP MF_01201		PRO_0000114496
Sites
	Active site	33	1	Proton acceptor; specific for D-alanine By similarity
	Active site	236	1	Proton acceptor; specific for L-alanine By similarity
Amino acid modifications
	Modified residue	33	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RER4-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B90B63A00C0EE1EF	FASTA	341	39,014
	10 20 30 40 50 60 MRRAVLEILE ERIIHNVKEI HRFSGKRIIA VVKANAYGIG VREVSRILEG LEEVDAFAVA 70 80 90 100 110 120 CTQEGVELRE CGIKKKILIL GGILEEDVKL LEEYDLTPVI SDPEHLKVLK DRNIKFHVKY 130 140 150 160 170 180 DTGMGRLGFT NEIIKDPRVE GVMSHFSSPA DRNFSKLQIK RFEEILKNYE KVKYIHLESS 190 200 210 220 230 240 AGLIYRVPFT THVRVGLAIY GEKPLKDYPL EVKPALRLRA RLISVKELPE NYPVSYGRTY 250 260 270 280 290 300 ITKRKTKLGV VAFGYADGLM KTLSNRSFLI FEGRKVPIIG NITMDMTMVD LSGTEARTGD 310 320 330 340 WVYIVNEERS FTPLARDAGT IPYEIMCNLS RRVERLVIKK R

References

[1]	"Molecular cloning of an extremely thermostable alanine racemase from Aquifex pyrophilus and enzymatic characterization of the expressed protein." Kim S.S., Yu Y.G. J. Biochem. Mol. Biol. 33:82-88(2000) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF212103 Genomic DNA. Translation: AAF23014.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.1.1.1. 271525.
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

ALR_AQUPY

Accession

Primary (citable) accession number: Q9RER4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 53 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)