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C6ED72

- C6ED72_ECOBD

UniProt

C6ED72 - C6ED72_ECOBD

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Protein
Alanine racemase
Gene
alr, B21_03885, ECBD_3980, ECD_03925
Organism
Escherichia coli (strain B / BL21-DE3)
Status
Unreviewed - Annotation score: 3 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 sitei34 – 341Proton acceptor; specific for D-alanine By similarityUniRule annotation
Binding sitei129 – 1291Substrate By similarityUniRule annotation
Active sitei255 – 2551Proton acceptor; specific for L-alanine By similarityUniRule annotation
Binding sitei303 – 3031Substrate; 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

UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation)
Gene namesi
Name:alrImported
Ordered Locus Names:B21_03885Imported, ECBD_3980Imported, ECD_03925Imported
OrganismiEscherichia coli (strain B / BL21-DE3)
Taxonomic identifieri469008 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001509: Chromosome, UP000009074: Chromosome, UP000002032: Chromosome

PTM / Processingi

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi469008.ECBD_3980.

Structurei

3D structure databases

ProteinModelPortaliC6ED72.
SMRiC6ED72. Positions 1-359.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0787.
HOGENOMiHOG000031446.
KOiK01775.
OMAiLWQLEAI.

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.

C6ED72-1 [UniParc]FASTAAdd to Basket

« Hide

MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP    50
DADAFGVARL EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH 100
NEEQLAALEE ASLDEPVTVW MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV 150
RQPVNIVSHF ARADEPKCGA TEKQLAIFNT FCEGKPGQRS IAASGGILLW 200
PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS LIAVREHKAG 250
EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR 300
VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT 350
SRVAMKYVD 359
Length:359
Mass (Da):39,153
Last modified:September 1, 2009 - v1
Checksum:iFDE9B438115342C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001665 Genomic DNA. Translation: ACT30965.1.
CP001509 Genomic DNA. Translation: ACT45716.1.
AM946981 Genomic DNA. Translation: CAQ34402.1.
RefSeqiYP_003001612.1. NC_012892.2.
YP_003038150.1. NC_012947.1.
YP_003056487.1. NC_012971.2.

Genome annotation databases

EnsemblBacteriaiACT30965; ACT30965; ECBD_3980.
ACT45716; ACT45716; ECD_03925.
CAQ34402; CAQ34402; B21_03885.
GeneIDi8114538.
8156653.
8179722.
KEGGiebd:ECBD_3980.
ebe:B21_03885.
ebl:ECD_03925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001665 Genomic DNA. Translation: ACT30965.1 .
CP001509 Genomic DNA. Translation: ACT45716.1 .
AM946981 Genomic DNA. Translation: CAQ34402.1 .
RefSeqi YP_003001612.1. NC_012892.2.
YP_003038150.1. NC_012947.1.
YP_003056487.1. NC_012971.2.

3D structure databases

ProteinModelPortali C6ED72.
SMRi C6ED72. Positions 1-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 469008.ECBD_3980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACT30965 ; ACT30965 ; ECBD_3980 .
ACT45716 ; ACT45716 ; ECD_03925 .
CAQ34402 ; CAQ34402 ; B21_03885 .
GeneIDi 8114538.
8156653.
8179722.
KEGGi ebd:ECBD_3980.
ebe:B21_03885.
ebl:ECD_03925.

Phylogenomic databases

eggNOGi COG0787.
HOGENOMi HOG000031446.
KOi K01775.
OMAi LWQLEAI.

Enzyme and pathway databases

UniPathwayi UPA00042 ; UER00497 .

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

« Hide 'large scale' publications
  1. "Sequencing and gene expression analysis of Escherichia coli BL21(DE3)."
    Krempl P.M., Mairhofer J., Eisenkolb M., Specht T., Leparc G.G., Kreil D.P., Bayer K., Striedner G.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Korea] and BL21Imported.
  3. "Sequencing and gene expression analysis of Escherichia coli BL21."
    Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
    Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Austria].
  4. "Complete sequence of Escherichia coli 'BL21-Gold(DE3)pLysS AG'."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21-GoldImported.
  5. "Complete sequence of Escherichia coli BL21(DE3)."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [JGI].
  6. Jeong H., Shim J.-H., Studier F.W., Oh T.K., Kim J.F.
    Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21.

Entry informationi

Entry nameiC6ED72_ECOBD
AccessioniPrimary (citable) accession number: C6ED72
Secondary accession number(s): C5WBT5
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: September 3, 2014
This is version 45 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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