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P10725 (ALR1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine racemase 1

EC=5.1.1.1
Gene names
Name:alr1
Synonyms:alr, dal
Ordered Locus Names:BSU04640
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. 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.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 389389Alanine racemase 1 HAMAP-Rule MF_01201
PRO_0000114500

Sites

Active site411Proton acceptor; specific for D-alanine By similarity
Active site2661Proton acceptor; specific for L-alanine By similarity
Binding site1371Substrate By similarity
Binding site3131Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict401V → E in AAA22378. Ref.1
Sequence conflict661V → M in AAA22378. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P10725 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 4802B7C182ACCD58

FASTA38943,265
        10         20         30         40         50         60 
MSTKPFYRDT WAEIDLSAIK ENVSNMKKHI GEHVHLMAVV KANAYGHGDA ETAKAALDAG 

        70         80         90        100        110        120 
ASCLAVAILD EAISLRKKGL KAPILVLGAV PPEYVAIAAE YDVTLTGYSV EWLQEAARHT 

       130        140        150        160        170        180 
KKGSLHFHLK VDTGMNRLGV KTEEEVQNVM AILDRNPRLK CKGVFTHFAT ADEKERGYFL 

       190        200        210        220        230        240 
MQFERFKELI APLPLKNLMV HCANSAAGLR LKKGFFNAVR FGIGMYGLRP SADMSDEIPF 

       250        260        270        280        290        300 
QLRPAFTLHS TLSHVKLIRK GESVSYGAEY TAEKDTWIGT VPVGYADGWL RKLKGTDILV 

       310        320        330        340        350        360 
KGKRLKIAGR ICMDQFMVEL DQEYPPGTKV TLIGRQGDEY ISMDEIAGRL ETINYEVACT 

       370        380 
ISSRVPRMFL ENGSIMEVRN PLLQVNISN 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of an alanine racemase gene from Bacillus subtilis and its use for plasmid maintenance in B. subtilis."
Ferrari E., Henner D.J., Yang M.Y.
Biotechnology (N.Y.) 3:1003-1007(1985)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus subtilis genome."
Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16207 Genomic DNA. Translation: AAA22378.1.
AB001488 Genomic DNA. Translation: BAA19301.1.
AL009126 Genomic DNA. Translation: CAB12271.1.
PIRJS0443.
RefSeqNP_388345.1. NC_000964.3.

3D structure databases

ProteinModelPortalP10725.
SMRP10725. Positions 4-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU04640.

Proteomic databases

PaxDbP10725.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12271; CAB12271; BSU04640.
GeneID939942.
KEGGbsu:BSU04640.
PATRIC18972512. VBIBacSub10457_0484.

Organism-specific databases

GenoListBSU04640. [Micado]

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAITMDQLM.
OrthoDBEOG6PP9NJ.
ProtClustDBCLSK886745.

Enzyme and pathway databases

BioCycBSUB:BSU04640-MONOMER.
SABIO-RKP10725.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SMARTSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMSSF50621. SSF50621. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR1_BACSU
AccessionPrimary (citable) accession number: P10725
Secondary accession number(s): P96620
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 15, 1998
Last modified: February 19, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList