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D1A324 (D1A324_THECD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 37. Feed History...

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

Sequence length375 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

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 site351Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2641Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1331Substrate By similarity HAMAP-Rule MF_01201
Binding site3121Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
D1A324 [UniParc].

Last modified January 19, 2010. Version 1.
Checksum: 94E4B931C926E1E8

FASTA37539,355
        10         20         30         40         50         60 
MREPVQARVD LDAIRANVAL LRERAGGAET MAMVKAEGYG HGLVEAARAA LEGGAGWLGV 

        70         80         90        100        110        120 
ARVAEALRLR AAGITVPVLV VMATRGEPFE EAVAAGVDLT AGSGWQARRL AEAAERAGRP 

       130        140        150        160        170        180 
ARVHLKADTG MSRGGATMAD WPATVEAALA AQAAGHLRVV GVMSHLACAD EPGHPSIARQ 

       190        200        210        220        230        240 
LAVFKEAVEY AEKAGVRPQV RHLSNSAATL TLPEARYDLV RPGIAIYGLT PVPQMGTFGL 

       250        260        270        280        290        300 
RPAMTLVAEL AAVKRVPAGS GVSYGHTYVT ERETTLGLVA AGYGDGVPRH GSSLLEVLAG 

       310        320        330        340        350        360 
GRRRRIAGRV CMDQFVIDLG DDTASPGEEV LLFGPGDHGE PTAQEWAQAL GTISYEIVTR 

       370 
IGTRVPRVYS GARWQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001738 Genomic DNA. Translation: ACY99794.1.
RefSeqYP_003301832.1. NC_013510.1.

3D structure databases

ProteinModelPortalD1A324.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACY99794; ACY99794; Tcur_4267.
GeneID8605623.
KEGGtcu:Tcur_4267.
PATRIC32518302. VBITheCur33965_4360.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.
OMAITMDQLM.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycTCUR471852:GHHD-4333-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.
[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.
ProtoNetSearch...

Entry information

Entry nameD1A324_THECD
AccessionPrimary (citable) accession number: D1A324
Entry history
Integrated into UniProtKB/TrEMBL: January 19, 2010
Last sequence update: January 19, 2010
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)