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

B1KTP9 (B1KTP9_CLOBM) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 52. 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 length404 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. HAMAP-Rule MF_01201 RuleBase RU004247 SAAS SAAS009006

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS009006

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201 RuleBase RU004247

Sequence similarities

Belongs to the alanine racemase family. HAMAP-Rule MF_01201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site381Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2751Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1441Substrate By similarity HAMAP-Rule MF_01201
Binding site3281Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue381N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
B1KTP9 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 08F9BC365E395B72

FASTA40445,827
        10         20         30         40         50         60 
MFEHSRPAWI EINLDNLIHN MKEIRRVARS KEIISVVKAD AYGHGALEIA SLLLENGANR 

        70         80         90        100        110        120 
LAVAVLSEAL ELRNNGITAP IIILGYTPLR YDEKTICNNA ETIIKNDLEV SVSSYKYAEQ 

       130        140        150        160        170        180 
LSKKAQQLGK DVKIHVNIDT GMGRLGFLPT EENLEKIYQI SKLPNIIFEG LFSHFSTADE 

       190        200        210        220        230        240 
KNKDYTNEQF KKFLDFYYKL RDKNVKVNIK HIANSAALID LPYTHLDAVR PGIAQYGYYP 

       250        260        270        280        290        300 
SSEVNHKDIN LRPIMTLKTN IVLVKDIKSG QSISYGRKFR TIRNSKIAVL PIGYADGYER 

       310        320        330        340        350        360 
ELSNENNVYK AQVIVNGRRA PIVGRITMDM CMIDVTDIGD VKVGDEVILI GECNDERISV 

       370        380        390        400 
EDIADLLNTI PYEVTSRISK RIPRYYMKDG KIVKISQINK EVNK 

« Hide

References

[1]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Loch Maree / Type A3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000962 Genomic DNA. Translation: ACA53599.1.
RefSeqYP_001785612.1. NC_010520.1.

3D structure databases

ProteinModelPortalB1KTP9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498214.CLK_3463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA53599; ACA53599; CLK_3463.
GeneID6152627.
KEGGcbl:CLK_3463.
PATRIC19385945. VBICloBot822_0593.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMARDLELCS.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycCBOT498214:GH05-316-MONOMER.
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 nameB1KTP9_CLOBM
AccessionPrimary (citable) accession number: B1KTP9
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)