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Protein

Alanine racemase

Gene

alr

Organism
Corynebacterium diphtheriae (strain VA01)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.UniRule annotation

Catalytic activityi

L-alanine = D-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341Proton acceptor; specific for D-alanineUniRule annotation
Binding sitei134 – 1341SubstrateUniRule annotation
Active sitei261 – 2611Proton acceptor; specific for L-alanineUniRule annotation
Binding sitei309 – 3091Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

  1. alanine racemase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-alanine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotationSAAS annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciCDIP698971:GHYD-472-MONOMER.
UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation)
Gene namesi
Name:alrImported
Ordered Locus Names:CDVA01_0454Imported
OrganismiCorynebacterium diphtheriae (strain VA01)Imported
Taxonomic identifieri698971 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000007155: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-(pyridoxal phosphate)lysineUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliH2I5B7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.UniRule annotation

Phylogenomic databases

KOiK01775.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
InterProiIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.

Sequencei

Sequence statusi: Complete.

H2I5B7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLLETRISC EAIAANTRRL KDMVAPAQLM CVVKADGYNH GAPEVATVMA
60 70 80 90 100
RNGADQFGVA TLAEAHQLRD AGITLPILCW IWSPEQDFSA AIDRDIDLAA
110 120 130 140 150
VSMEHVRALI AEAMRRPAGT RVRVTVKIDT ELHRSGIDEA NWTEAFELLH
160 170 180 190 200
ACPQINVTGV FSHLACADDL ESDYTDHQAE VFRRAIDAGR RVGLDLSVNH
210 220 230 240 250
LAASPATLTR PDLHFDMVRP GLALYGHEPI AGLDHGLREA MTWIGSVTVV
260 270 280 290 300
KPIAAGQGTS YNMTWHAPAD GYLCVVPVGY ADGLPRNVQG HLEVTIAGTR
310 320 330 340 350
YPQVGRVCMD QIVVFLGDNS RGVAPGDEAI IFGPRDTQAM TVTELACATG
360 370 380
TINYEILCRP TGRSHRTYSA LDAVAPTHPT ES
Length:382
Mass (Da):41,337
Last modified:March 21, 2012 - v1
Checksum:i33AE57F1B1D9235A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003217 Genomic DNA. Translation: AEX82723.1.
RefSeqiYP_005144363.1. NC_016790.1.

Genome annotation databases

EnsemblBacteriaiAEX82723; AEX82723; CDVA01_0454.
GeneIDi11718942.
KEGGicdv:CDVA01_0454.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003217 Genomic DNA. Translation: AEX82723.1.
RefSeqiYP_005144363.1. NC_016790.1.

3D structure databases

ProteinModelPortaliH2I5B7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEX82723; AEX82723; CDVA01_0454.
GeneIDi11718942.
KEGGicdv:CDVA01_0454.

Phylogenomic databases

KOiK01775.

Enzyme and pathway databases

UniPathwayiUPA00042; UER00497.
BioCyciCDIP698971:GHYD-472-MONOMER.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
InterProiIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Pangenomic study of Corynebacterium diphtheriae that provides insights into the genomic diversity of pathogenic isolates from cases of classical diphtheria, endocarditis, and pneumonia."
    Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., Santos C.S., Santos L.S., Hirata R. Jr.
    , Mattos-Guaraldi A.L., Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.
    J. Bacteriol. 194:3199-3215(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VA01Imported.

Entry informationi

Entry nameiH2I5B7_CORDV
AccessioniPrimary (citable) accession number: H2I5B7
Entry historyi
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: February 4, 2015
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.