A0R8V1 (A0R8V1_BACAH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Alanine racemase 1 HAMAP MF_01201
EC=5.1.1.1 HAMAP MF_01201

Gene names

Name:	alr EMBL ABK83644.1
Synonyms:	alr1 HAMAP MF_01201
Ordered Locus Names:	BALH_0237

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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
Molecular function	Isomerase SAAS SAAS009006 HAMAP MF_01201 RuleBase RU000608 EMBL ABK83644.1
Technical term	Complete proteome
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	41	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	41	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01201

Sequences

	Sequence		Length	Mass (Da)
	A0R8V1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: E26E7ACCAA096FAD	FASTA	389	43,650
	10 20 30 40 50 60 MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSDVEIFAVV KGNAYGHDYV PVAKTALEAG 70 80 90 100 110 120 ATRLAVAFLD EALVLRRAGI TAPILVLGPS PPRDINVAAE NDVALTVFQK EWVDEAIKLW 130 140 150 160 170 180 DGSSTMKYHI NFDSGMGRIG IRERKELKGF LKSLEGAPFL ELEGVYTHFA TADEVETSYF 190 200 210 220 230 240 DKQYNTFLEQ LSWLKEFGVD PKFVHTANSA ATLRFQGITF NAVRIGIAMY GLSPSVEIRP 250 260 270 280 290 300 FLPFKLEPAL SLHTKVAHIK QVIKGDGISY NVTYRTKTEE WIATVAIGYA DGWLRRLQGF 310 320 330 340 350 360 EVLVNGKRVP IVGRVTMDQF MIHLPCEVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE 370 380 IITTISFRVP RIFIRNGKVV EVINYLNDI

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000485 Genomic DNA. Translation: ABK83644.1.
RefSeq	YP_893151.1. NC_008600.1.
3D structure databases
ProteinModelPortal	A0R8V1.
SMR	A0R8V1. Positions 4-389.
ModBase	Search...
Protein-protein interaction databases
STRING	A0R8V1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000071031; EBBACP00000069268; EBBACG00000071022.
GeneID	4546571.
GenomeReviews	Gene locus BALH_0237 in contig CP000485_GR.
KEGG	btl:BALH_0237.
PATRIC	18992509. VBIBacThu63319_0331.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0787.
GeneTree	EBGT00050000001615.
HOGENOM	HBG712172.
OMA	TRKEDAN.
ProtClustDB	CLSK915752.
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.
KO	K01775.
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

A0R8V1_BACAH

Accession

Primary (citable) accession number: A0R8V1

Entry history

Integrated into UniProtKB/TrEMBL:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)