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F7X514

- F7X514_SINMM

UniProt

F7X514 - F7X514_SINMM

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Protein

Alanine racemase

Gene
alr, SM11_chr2537
Organism
Sinorhizobium meliloti (strain SM11)
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 sitei54 – 541Proton acceptor; specific for D-alanine By similarityUniRule annotation
Binding sitei151 – 1511Substrate By similarityUniRule annotation
Active sitei273 – 2731Proton acceptor; specific for L-alanine By similarityUniRule annotation
Binding sitei332 – 3321Substrate; 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 annotations

Keywords - Ligandi

Pyridoxal phosphateUniRule annotationSAAS annotations

Enzyme and pathway databases

BioCyciSMEL707241:GLKB-2536-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:SM11_chr2537Imported
OrganismiSinorhizobium meliloti (strain SM11)Imported
Taxonomic identifieri707241 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000009045: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-(pyridoxal phosphate)lysine By similarityUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliF7X514.

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.

F7X514-1 [UniParc]FASTAAdd to Basket

« Hide

MYCCRYRPRR VFGMQSPEFL SASSRLTVDL TALADNWRAM NERSGKARAA    50
AVLKADAYGL GVVHAAPALY AAGARDFFVA SVEEGADLRP LVPDGRIYIL 100
AGMWPGNEEL FFENDLVPII NSEEQLAVFM AALSERGDHP CVLHVDTGMN 150
RLGLSPEEAL ALAHDPARPA SFSPVLVMSH LACADDPGHP MNRYQLQRFR 200
EVTAAFEGVP ASLANSGGVF LGADYHFDLT RPGIAVYGGE AVNGAVNPMK 250
AVVTAEARIV QVRTVPSGGT ASYGASVRFG RDSRIATVAI GYADGYHRSV 300
SGGGVTLRQA MPSGAFGFLH GMKVPHVGRV TMDLSLFDVT DLPEAAVRAG 350
DYIEVFGRNV VIDDVARAGG TIGYELLTSL GRRYHRTYVG GA 392
Length:392
Mass (Da):41,923
Last modified:September 21, 2011 - v1
Checksum:iD8D9511570C83B50
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001830 Genomic DNA. Translation: AEH79790.1.
RefSeqiYP_005721051.1. NC_017325.1.

Genome annotation databases

EnsemblBacteriaiAEH79790; AEH79790; SM11_chr2537.
GeneIDi12310982.
KEGGismx:SM11_chr2537.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001830 Genomic DNA. Translation: AEH79790.1 .
RefSeqi YP_005721051.1. NC_017325.1.

3D structure databases

ProteinModelPortali F7X514.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEH79790 ; AEH79790 ; SM11_chr2537 .
GeneIDi 12310982.
KEGGi smx:SM11_chr2537.

Phylogenomic databases

KOi K01775.

Enzyme and pathway databases

UniPathwayi UPA00042 ; UER00497 .
BioCyci SMEL707241:GLKB-2536-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. "The complete genome sequence of the dominant Sinorhizobium meliloti field isolate SM11 extends the S. meliloti pan-genome."
    Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H., Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.
    J. Biotechnol. 155:20-33(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SM11Imported.

Entry informationi

Entry nameiF7X514_SINMM
AccessioniPrimary (citable) accession number: F7X514
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: July 9, 2014
This is version 23 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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