Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B3PK19 (B3PK19_CELJU) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 53. 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

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. 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site491Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2721Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1471Substrate By similarity HAMAP-Rule MF_01201
Binding site3201Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue491N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
B3PK19 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 3ACEF92858320C29

FASTA37941,308
        10         20         30         40         50         60 
MIHHPSPDLL PAMITSSGIL TIDLHAICAN WHFLKNQVAP HVDVAAVVKA NAYGLGAVPV 

        70         80         90        100        110        120 
VRALRKEGCT TFFFATKEEA LASGLNGEHC LKIVLSGVRS GDEPFFVEGQ LTPVLYSLAD 

       130        140        150        160        170        180 
VQRWNAYAKN CCKRLPCILK VDTGMTRMGM SIEELEAFCE AHASIHIAPL FLMSHLACAD 

       190        200        210        220        230        240 
TPSHPANQRQ LQLFKQALDI AQVRFPEIKA SLANSAGILL GADWHFDLVR PGAALYGINP 

       250        260        270        280        290        300 
VSGIPNLLKP VITLSLPVLQ IRSLQHDAYV GYSATHFAKA GSRLAVVAGG YADGIHRTLG 

       310        320        330        340        350        360 
FKPLAQFNGM AFEAVGRVSM DSCVFDISQC PENRLPQVGD YLEVVNESLS LNFLMERNAS 

       370 
LGYEVLNSLG TRFHRIYQE 

« Hide

References

[1]"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107 EMBL ACE84020.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000934 Genomic DNA. Translation: ACE84020.1.
RefSeqYP_001981190.1. NC_010995.1.

3D structure databases

ProteinModelPortalB3PK19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498211.CJA_0676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE84020; ACE84020; CJA_0676.
GeneID6416117.
KEGGcja:CJA_0676.
PATRIC21324725. VBICelJap122165_0673.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031445.
KOK01775.
OMAPAGVCWR.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-676-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 nameB3PK19_CELJU
AccessionPrimary (citable) accession number: B3PK19
Entry history
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: July 9, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)