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I3TLS5 (I3TLS5_TISMK) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 15. Feed History...

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

Sequence length408 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 SAAS SAAS020622

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS020622

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site521Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2801Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1581Substrate By similarity HAMAP-Rule MF_01201
Binding site3281Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue521N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
I3TLS5 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: DDE662A4BEFA99E0

FASTA40842,856
        10         20         30         40         50         60 
MSTPLTALPA APAAPPPAWI EIDLDALAEN HARLTGLMRA HNPAAEVTGV IKADGYGLGA 

        70         80         90        100        110        120 
DIVGPALARA GAPALFVAHL SEGAALRRAL RADPDPARHA LPVYILNGMA EGERADFLAF 

       130        140        150        160        170        180 
DLRPVLNGPD DLDRWTRAGQ AQGGPLPAAL HIDTGMSRLG FDEAGFKALA ADPARLGGVD 

       190        200        210        220        230        240 
IRITMSHLAC ADDPAHPLNR RQLDRFRAVT AVVGRGRLSL ANSSGLFLGP DFHFDLGRPG 

       250        260        270        280        290        300 
VALYGVNPVP GHPNPMVPVV RLKARVLQVR TIDSFESVGY GAAARARPGM RVATLAIGYA 

       310        320        330        340        350        360 
DGWPWSAAGK GEVVIAGHRA PILGRVSMDL VTVDVSTLPE PLIHGGAVAE LIGDHRDIDA 

       370        380        390        400 
LAKDAGTIGY EILTRLGRRY ARQPMTSGQT QVYPIGVPTP QTEVDPAP 

« Hide

References

[1]"Bacterial biosynthesis and maturation of the didemnin anti-cancer agents."
Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H., Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.
J. Am. Chem. Soc. 134:8625-8632(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KA081020-065 EMBL AFK53713.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003236 Genomic DNA. Translation: AFK53713.1.
RefSeqYP_006371297.1. NC_017956.1.

3D structure databases

ProteinModelPortalI3TLS5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFK53713; AFK53713; TMO_1874.
GeneID13004988.
KEGGtmo:TMO_1874.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01775.
OMAMNLDMVR.

Enzyme and pathway databases

BioCycTMOB1110502:GLMJ-1893-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.
IPR020622. Ala_racemase_pyridoxalP-BS.
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.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI3TLS5_TISMK
AccessionPrimary (citable) accession number: I3TLS5
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: July 9, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)