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H9ZTH0 (H9ZTH0_THETH) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Alanine racemase HAMAP-Rule MF_01201

EC=5.1.1.1 HAMAP-Rule MF_01201
Gene names
ORF Names:TtJL18_1761 EMBL AFH39630.1
OrganismThermus thermophilus JL-18 [Complete proteome] EMBL AFH39630.1
Taxonomic identifier798128 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 SAAS001608

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site431Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2561Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1411Substrate By similarity HAMAP-Rule MF_01201
Binding site3031Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue431N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
H9ZTH0 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 1122843A02FEF2DF

FASTA36038,856
        10         20         30         40         50         60 
MRPRGYPKGV QARAWIEVDL AALWANYRLL AGRAGGEVIP VLKADAYGHG ALPLARFLEG 

        70         80         90        100        110        120 
KGVGRFAVAT LEEGRRLREG GIKGEVLLLG SLHPLEAEEA LELGLVPTLS TLEAAEALSL 

       130        140        150        160        170        180 
RARALGLVPR AHLKVDTGMN RVGFPWEEAA SALRAVEAMG VRVEGVYTHL ATAGEDAAFV 

       190        200        210        220        230        240 
ETQRRRFQEV RRALGENYFY HLENSLGLLR HGATAGVRVG LALYGLVPGF GLRPILRILA 

       250        260        270        280        290        300 
RPTLVKRLKA GDRVGYGGVY VARGGEWLAT LPVGYADGLP WGAVRFVKGP DGRLLEVAGR 

       310        320        330        340        350        360 
ISMDQTTVLL PGPVGLEAVF EVLSADFGPT GLLAWAEARG TLPYEVAVHL SRRLPRRYLE 

« Hide

References

[1]US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lam J. expand/collapse author list , McDonald A., Dodsworth J., Hedlund B., Woyke T.
Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: JL-18 EMBL AFH39630.1.
[2]"Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus JL-18, Incomplete Denitrifiers from the United States Great Basin."
Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S., Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I., Dodsworth J.A. expand/collapse author list , Pati A., Goodwin L., Peters L., Pitluck S., Woyke T., Hedlund B.P.
Genome Announc. 1:E00106-E00112(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: JL-18 EMBL AFH39630.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003252 Genomic DNA. Translation: AFH39630.1.
RefSeqYP_006059416.1. NC_017587.1.

3D structure databases

ProteinModelPortalH9ZTH0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFH39630; AFH39630; TtJL18_1761.
GeneID12654435.
KEGGttl:TtJL18_1761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01775.

Enzyme and pathway databases

BioCycTTHE798128:GLMF-1760-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR029066. PLP-binding_barrel.
[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.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameH9ZTH0_THETH
AccessionPrimary (citable) accession number: H9ZTH0
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: July 9, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)