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E4TW12 (E4TW12_MARTH) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length395 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 SAAS SAAS009006

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS009006

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. HAMAP-Rule MF_01201 RuleBase RU004188

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site401Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2871Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1391Substrate By similarity HAMAP-Rule MF_01201
Binding site3351Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue401N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E4TW12 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 647D0232B79687CE

FASTA39544,758
        10         20         30         40         50         60 
MNQSIFSTST ITLSKSAVRQ NVRFVRKRLA ENVLLSAVLK GNAYGHGIKG MVPLFESANV 

        70         80         90        100        110        120 
KHLSVFSTHE AEQVCQVKKK TTEVMIMGWM EDEETEWAIE NEVEFYVFEM GRLKAALHYA 

       130        140        150        160        170        180 
KTLNKIAKIH VEVETGMNRT GFEEEHLEEL MQMMKENHEY ISFVGLCTHY AGAESITNYL 

       190        200        210        220        230        240 
RVVDQIKKYK KIYDLFVEND LVPKRRHTAC SAAAMSYPET QMDMVRIGIL LYGFWPSQET 

       250        260        270        280        290        300 
FIAYQRSNGH GQDGLDRKVR HPLKRVISWR SKIMSVKEVP VGEFIGYGTS YQATKKMKIA 

       310        320        330        340        350        360 
TVPVGYAYGF ARSLSNQGRV IVNGKRVAVI STVNMNLMII NVTECKNVGK GDEVIMIGSN 

       370        380        390 
GKVNVTVASF GELSNQLNYE LLSRLPMDIP RRVVI 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002349 Genomic DNA. Translation: ADR23230.1.
RefSeqYP_004055338.1. NC_014759.1.

3D structure databases

ProteinModelPortalE4TW12.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADR23230; ADR23230; Ftrac_3256.
GeneID10013414.
KEGGmtt:Ftrac_3256.
PATRIC45219957. VBIMarTra126157_3365.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000166881.
KOK01775.

Enzyme and pathway databases

BioCycMTRA643867:GI2X-3299-MONOMER.
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 nameE4TW12_MARTH
AccessionPrimary (citable) accession number: E4TW12
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: February 19, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)