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D3DHB2 (D3DHB2_HYDTT) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 39. Feed History...

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

Sequence length338 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. SAAS SAAS009006 HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS009006 HAMAP-Rule MF_01201

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. RuleBase RU004188 HAMAP-Rule MF_01201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site331Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2361Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1261Substrate By similarity HAMAP-Rule MF_01201
Binding site2841Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue331N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
D3DHB2 [UniParc].

Last modified March 23, 2010. Version 1.
Checksum: DD077B82BA883592

FASTA33837,315
        10         20         30         40         50         60 
MARAVLEIDA DAIRQNIKAI RDFSGKRVIA VVKADAYGIG AVHICPILEA LDEVSSFAVA 

        70         80         90        100        110        120 
CVEEGIELRK AGIKKDILIL GGVFKGERKA LIEYALTPVV SHEAHLRAIE GLDIGFHVKY 

       130        140        150        160        170        180 
DTGMGRLGFF EDVLIKDRRV KGVLTHLSSP LDKDFSLMQI EKFKKIVKAY SNVDIHLESS 

       190        200        210        220        230        240 
AGIVYMVPFA THVRIGLAMY GEKPAPDYPI ELKRAISIKA RILSVKYLPP SYPVSYSRTF 

       250        260        270        280        290        300 
ITDRKKKVGV VAFGYADGLA KALSNVGCLY WKDKPLRILG NITMDMTMVD LDDTDAQVGD 

       310        320        330 
EVEVVGPHQS FSHLAKLAGT IPYEIMCHLS SRIKRVVV 

« Hide

References

[1]"Complete genome sequence of the thermophilic, obligately chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter thermophilus TK-6."
Arai H., Kanbe H., Ishii M., Igarashi Y.
J. Bacteriol. 192:2651-2652(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6534 / IAM 12695 / TK-6 [Tokyo] and TK-6.
[2]"Complete genome sequence of Hydrogenobacter thermophilus type strain (TK-6)."
US DOE Joint Genome Institute (JGI-PGF)
Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A. expand/collapse author list , Palaniappan K., Ngatchou O., Land M., Hauser L., Chang Y., Jeffries C., Han C., Detter J., Ubler S., Rohde M., Tindall B., Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.
Stand. Genomic Sci. 4:131-143(2011)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6534 / IAM 12695 / TK-6 [JGI] and TK-6 EMBL ADO45151.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002221 Genomic DNA. Translation: ADO45151.1.
AP011112 Genomic DNA. Translation: BAI69214.1.
RefSeqYP_003432415.1. NC_013799.1.
YP_005511444.1. NC_017161.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADO45151; ADO45151; Hydth_0754.
BAI69214; BAI69214; HTH_0754.
GeneID12100895.
8773948.
KEGGhte:Hydth_0754.
hth:HTH_0754.
PATRIC32210403. VBIHydThe36152_0761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.
OMAINNQLAP.

Enzyme and pathway databases

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 nameD3DHB2_HYDTT
AccessionPrimary (citable) accession number: D3DHB2
Entry history
Integrated into UniProtKB/TrEMBL: March 23, 2010
Last sequence update: March 23, 2010
Last modified: March 19, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)