Reviewed, UniProtKB/Swiss-Prot Q9FCV2 (ALR_LACRE)

Names and origin

Protein names

Recommended name:
    Alanine racemase
    EC=5.1.1.1

Gene names

Name:

alr

Organism

Lactobacillus reuteri

Taxonomic identifier

1598 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
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
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 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 – 375	375	Alanine racemase HAMAP MF_01201		PRO_0000114529
Sites
	Active site	40	1	Proton acceptor; specific for D-alanine By similarity
	Active site	265	1	Proton acceptor; specific for L-alanine By similarity
Amino acid modifications
	Modified residue	40	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9FCV2-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 2912040451188DEB	FASTA	375	41,248
	10 20 30 40 50 60 MVEGWHRASR LVVDAAAIRQ NVKKEIERLD PQSELFAVVK ANGYGHGLIP VARYTEQAGA 70 80 90 100 110 120 TGFCVAILDE ALTLREAGFA EPILVLGITN VKWAALAAEK NVSLTVGDVE WLTKAAPQLT 130 140 150 160 170 180 AEHPLKVHLA LDTGMGRIGF QESDGLNQAA ELLTNDPRFV FEGVFTHFAT ADEKDPTYFN 190 200 210 220 230 240 LQVDRFHKLV DTLPEKPRYV HVSNTATSLW HAACNGNLIR FGVGIYGMNP SGTVLEPPYD 250 260 270 280 290 300 LQPAMTLESQ LSFSKLLKKG RSVSYGATYT VEQDEWIGTV PIGYADGYPR CLQGFHVLVD 310 320 330 340 350 360 GHFCEIVGRV CMDQLMIRLP HEYPAGTSVI LAGKSQGKSI SMTDIADYAG TINYEITCGF 370 TERIPRVYKN NDIVK

References

[1]	"Characterization of an alanine racemase gene from Lactobacillus reuteri." Thompson A., Griffin H., Gasson M.J. Curr. Microbiol. 44:246-250(2002) [PubMed: 11910493] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 53608 / 1063.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ278312 Genomic DNA. Translation: CAC03497.1.
3D structure databases
HSSP	HSSP built from PDB template 1BD0 based on UniProtKB P10724.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.1.1.1. 20849.
Family and domain databases
HAMAP	MF_01201. [Tree]
InterPro	IPR011079. Ala_racemase_C. IPR001608. Ala_racemase_N. IPR000821. Ala_racemase_reg. [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_LACRE

Accession

Primary (citable) accession number: Q9FCV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 1, 2001
Last modified:	May 26, 2009
This is version 50 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)