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C7T794 (C7T794_LACRG) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 44. 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 attributes

Sequence length379 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. RuleBase RU004247 HAMAP-Rule MF_01201 SAAS SAAS020622

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS020622 HAMAP-Rule MF_01201

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. RuleBase RU004247 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 site401Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2701Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1401Substrate By similarity HAMAP-Rule MF_01201
Binding site3171Substrate; 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
C7T794 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: F3DB8FE136716B0B

FASTA37941,267
        10         20         30         40         50         60 
MTIGNLRPAT VLIDETAILH NVQHEVARLK KQTQLFAVVK ADAYGHGMLR VAHVAKAAGA 

        70         80         90        100        110        120 
SGFCVALLDE ALDLRAANYT EPVLVLGIVP SQYAAIAAAQ TVSLPLSSVD WLKQALPVLE 

       130        140        150        160        170        180 
AQPELPPLRL HIALDTGMGR IGFTDDQTLL DAVAFIQAHP KAFTIEGIFT HFATADDPDD 

       190        200        210        220        230        240 
AYFKQQVAKF NHMVALLPHR PRYVHVSNSA TSLWHAACNG NMVRYGVAIY GLNPSGDVIP 

       250        260        270        280        290        300 
TTPFPLEPAL SLESELTFCK QVHAGDGISY GVTYRATGDE FIGTVPVGYA DGWLRRLQGF 

       310        320        330        340        350        360 
HVLVDGHLCE IVGRICMDQF MIRLPKAYPA GTKVVLIGQS GDQEITLLDV AKYSHTIHYE 

       370 
IACNLTSRLK RQSINPIAR 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the probiotic Lactobacillus rhamnosus ATCC 53103."
Morita H., Toh H., Oshima K., Murakami M., Taylor T.D., Igimi S., Hattori M.
J. Bacteriol. 191:7630-7631(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53103 EMBL BAI42960.1 and ATCC 53103 / GG [Tokyo].
[2]"Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human- mucus binding protein."
Kankainen M., Paulin L., Tynkkynen S., von Ossowski I., Reunanen J., Partanen P., Satokari R., Vesterlund S., Hendrickx A.P., Lebeer S., De Keersmaecker S.C., Vanderleyden J., Hamalainen T., Laukkanen S., Salovuori N., Ritari J., Alatalo E., Korpela R. expand/collapse author list , Mattila-Sandholm T., Lassig A., Hatakka K., Kinnunen K.T., Karjalainen H., Saxelin M., Laakso K., Surakka A., Palva A., Salusjarvi T., Auvinen P., de Vos W.M.
Proc. Natl. Acad. Sci. U.S.A. 106:17193-17198(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53103 / GG [Helsinki].
[3]"Genomic Adaptation of the Lactobacillus casei Group."
Toh H., Oshima K., Nakano A., Takahata M., Murakami M., Takaki T., Nishiyama H., Igimi S., Hattori M., Morita H.
PLoS ONE 8:e75073-e75073(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 53103 EMBL BAI42960.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP011548 Genomic DNA. Translation: BAI42960.1.
FM179322 Genomic DNA. Translation: CAR88431.1.
RefSeqYP_003172282.1. NC_013198.1.
YP_005866925.1. NC_017482.1.

3D structure databases

ProteinModelPortalC7T794.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING568703.LGG_02536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI42960; BAI42960; LRHM_2433.
CAR88431; CAR88431; LGG_02536.
GeneID12475585.
8421609.
KEGGlrg:LRHM_2433.
lrh:LGG_02536.
PATRIC22266296. VBILacRha2892_2404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAYGHGLER.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycLRHA568703:GCGS-2502-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 nameC7T794_LACRG
AccessionPrimary (citable) accession number: C7T794
Secondary accession number(s): C8UX56
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: July 9, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)