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K0MFB9 (K0MFB9_BORPB) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 12. Feed History...

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

Sequence length387 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. SAAS SAAS020622 HAMAP-Rule MF_01201

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

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 site1441Substrate 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
K0MFB9 [UniParc].

Last modified November 28, 2012. Version 1.
Checksum: 706F846FF0EF2A75

FASTA38741,465
        10         20         30         40         50         60 
MPLASDPFDA PIPGLHACID PIAVAHNLEV LRQRLGVGVD GPRIWATVKA DAYGHGLHNV 

        70         80         90        100        110        120 
LPGLRAADGI AVRHLHEAHQ CRRVGWRGPI MVYAGLTHER EAALLTLQQL HLVITDMTQL 

       130        140        150        160        170        180 
EWLPGKPLYA CAPWVWLRYI GATRLGGLDA GEYRRAYARC RELQQHGALR GVGHLNHYAN 

       190        200        210        220        230        240 
AASVGDLERE HADFEACIRG LPGPVSTCNS AASCVMPTMA ARTDWVRPGL ALYGVSPIPD 

       250        260        270        280        290        300 
RVGRDLGLRP AMTLRSTLCA TQKLPAGASV GYGCAFVADQ PMALGLVRCG YGDGYPHNPR 

       310        320        330        340        350        360 
ASFPVQVDGV LTRTVGRISM DLMAVDLRPI PAAARGAPVV LWGSPQLPVE HIAHAADTIA 

       370        380 
AELLTGLTAR VPLMRADHAA LLRGPLA 

« Hide

References

[1]"Comparative genomics of the classical Bordetella subspecies: the evolution and exchange of virulence-associated diversity amongst closely related pathogens."
Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M., Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.
BMC Genomics 13:545-545(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bpp5 EMBL CCJ48739.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE965803 Genomic DNA. Translation: CCJ48739.1.
RefSeqYP_006895388.1. NC_018828.1.

3D structure databases

ProteinModelPortalK0MFB9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCJ48739; CCJ48739; BN117_1406.
GeneID13889442.
KEGGbpar:BN117_1406.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01775.

Enzyme and pathway databases

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 nameK0MFB9_BORPB
AccessionPrimary (citable) accession number: K0MFB9
Entry history
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: July 9, 2014
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)