C6ED72 (C6ED72_ECOBD) 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 ACT45716.1
Ordered Locus Names:	B21_03885, ECBD_3980, ECD_03925

Organism

Escherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]

Taxonomic identifier

469008 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	359 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. HAMAP-Rule MF_01201
Catalytic activity	L-alanine = D-alanine. SAAS SAAS020622 HAMAP-Rule MF_01201
Cofactor	Pyridoxal phosphate By similarity. SAAS SAAS020622 HAMAP-Rule MF_01201
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. RuleBase RU004188 HAMAP-Rule MF_01201

Ontologies

Keywords
Ligand	Pyridoxal phosphate SAAS SAAS020622 HAMAP-Rule MF_01201
Molecular function	Isomerase SAAS SAAS020622 HAMAP-Rule MF_01201 EMBL ACT30965.1
Technical term	Complete 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	34	1	Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
	Active site	255	1	Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
	Binding site	129	1	Substrate By similarity HAMAP-Rule MF_01201
	Binding site	303	1	Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201
Amino acid modifications
	Modified residue	34	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

	Sequence		Length	Mass (Da)
	C6ED72 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: FDE9B438115342C2	FASTA	359	39,153
	10 20 30 40 50 60 MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL 70 80 90 100 110 120 EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW 130 140 150 160 170 180 MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT 190 200 210 220 230 240 FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS 250 260 270 280 290 300 LIAVREHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR 310 320 330 340 350 VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD

References

[1]	"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)." Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F. J. Mol. Biol. 394:644-652(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B / BL21-DE3 [Korea].
[2]	"Sequencing and gene expression analysis of Escherichia coli BL21." Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M. Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B / BL21-DE3 [Austria].
[3]	"Complete sequence of Escherichia coli BL21(DE3)." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E. Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B / BL21-DE3 [JGI].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001665 Genomic DNA. Translation: ACT30965.1. CP001509 Genomic DNA. Translation: ACT45716.1. AM946981 Genomic DNA. Translation: CAQ34402.1.
RefSeq	YP_003001612.1. NC_012892.2. YP_003038150.1. NC_012947.1. YP_003056487.1. NC_012971.2.
3D structure databases
SMR	C6ED72. Positions 1-359.
ModBase	Search...
Protein-protein interaction databases
STRING	469008.ECBD_3980.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACT30965; ACT30965; ECBD_3980. ACT45716; ACT45716; ECD_03925. CAQ34402; CAQ34402; B21_03885.
GeneID	8114538. 8156653. 8179722.
KEGG	ebd:ECBD_3980. ebe:B21_03885. ebl:ECD_03925.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0787.
HOGENOM	HOG000031446.
KO	K01775.
OMA	HQLETAV.
ProtClustDB	PRK00053.
Enzyme and pathway databases
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

C6ED72_ECOBD

Accession

Primary (citable) accession number: C6ED72
Secondary accession number(s): C5WBT5

Entry history

Integrated into UniProtKB/TrEMBL:	September 1, 2009
Last sequence update:	September 1, 2009
Last modified:	May 29, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)