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F2RJX4

- F2RJX4_STRVP

UniProt

F2RJX4 - F2RJX4_STRVP

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Protein
Alanine racemase
Gene
SVEN_4422
Organism
Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

L-alanine = D-alanine.UniRule annotationSAAS annotations

Cofactori

Pyridoxal phosphate By similarity.UniRule annotationSAAS annotations

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei41 – 411Proton acceptor; specific for D-alanine By similarityUniRule annotation
Binding sitei140 – 1401Substrate By similarityUniRule annotation
Active sitei274 – 2741Proton acceptor; specific for L-alanine By similarityUniRule annotation
Binding sitei322 – 3221Substrate; via amide nitrogen By similarityUniRule 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 annotationsImported

Keywords - Ligandi

Pyridoxal phosphateUniRule annotationSAAS annotations

Enzyme and pathway databases

BioCyciSVEN953739-WGS:GSXO-4491-MONOMER.
UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation)
Gene namesi
Ordered Locus Names:SVEN_4422Imported
OrganismiStreptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)Imported
Taxonomic identifieri953739 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
ProteomesiUP000006854: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-(pyridoxal phosphate)lysine By similarityUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliF2RJX4.

Family & Domainsi

Sequence similaritiesi

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.
IPR020622. Ala_racemase_pyridoxalP-BS.
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.
PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F2RJX4-1 [UniParc]FASTAAdd to Basket

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MTETPPPRRA RAEIDLGALR ANVRTLRARV APHVRIMAVV KADAYGHGAV    50
RCARAALDAG ADWLGTATPH EALALRAAGI TDVPVMCWLW TPGDPWDQGI 100
EAGLDMSVSG MWALEEVVRA ARATGGVARV QLKADTGLGR NGCQPADWPE 150
LVGEALKAEA EGLVEVTGLW SHFACADEPH HPSIAAQLDV FRSMLDYAEK 200
AGVRPEVRHI ANSPATLTLP EAHFDLVRPG IAMYGVSPSP ELGTSAELGL 250
RPVMSLKASV ALVKRVPAGH GVSYGHHYVT DAETTLGLVP LGYADGVPRH 300
ASGRGPVLVD GTVRTVAGRV AMDQFVVDLG GDVPAPGTEA VLFGPGDLGE 350
PTAEDWAVAA DTIAYEIVTR IGARVPRVYL GE 382
Length:382
Mass (Da):40,210
Last modified:May 31, 2011 - v1
Checksum:i354E8FA1AB2CC23D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FR845719 Genomic DNA. Translation: CCA57708.1.
RefSeqiWP_015035610.1. NC_018750.1.
YP_006879967.1. NC_018750.1.

Genome annotation databases

EnsemblBacteriaiCCA57708; CCA57708; SVEN_4422.
GeneIDi13819580.
KEGGisve:SVEN_4422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FR845719 Genomic DNA. Translation: CCA57708.1 .
RefSeqi WP_015035610.1. NC_018750.1.
YP_006879967.1. NC_018750.1.

3D structure databases

ProteinModelPortali F2RJX4.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CCA57708 ; CCA57708 ; SVEN_4422 .
GeneIDi 13819580.
KEGGi sve:SVEN_4422.

Phylogenomic databases

KOi K01775.

Enzyme and pathway databases

UniPathwayi UPA00042 ; UER00497 .
BioCyci SVEN953739-WGS:GSXO-4491-MONOMER.

Family and domain databases

Gene3Di 2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPi MF_01201. Ala_racemase.
InterProi IPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view ]
Pfami PF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view ]
PRINTSi PR00992. ALARACEMASE.
SMARTi SM01005. Ala_racemase_C. 1 hit.
[Graphical view ]
SUPFAMi SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR00492. alr. 1 hit.
PROSITEi PS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae provides new insights into global nitrogen regulation in actinomycetes."
    Pullan S.T., Chandra G., Bibb M.J., Merrick M.
    BMC Genomics 12:175-175(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745.

Entry informationi

Entry nameiF2RJX4_STRVP
AccessioniPrimary (citable) accession number: F2RJX4
Entry historyi
Integrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: September 3, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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