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P46397 (BIOD_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent dethiobiotin synthetase BioD
EC=6.3.3.3
Alternative name(s):
DTB synthetase
Short name=DTBS
Dethiobiotin synthase
Gene names
Name:bioD
Ordered Locus Names:Cgl2605, cg2886
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring By similarity. HAMAP MF_00336

Catalytic activity

ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin. HAMAP MF_00336

Cofactor

Magnesium.

Pathway

Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. HAMAP MF_00336

Subcellular location

Cytoplasm By similarity HAMAP MF_00336.

Sequence similarities

Belongs to the dethiobiotin synthetase family.

Ontologies

Keywords
   Biological processBiotin biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processbiotin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

dethiobiotin synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 224224ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000187960

Regions

Nucleotide binding107 – 1104ATP By similarity
Nucleotide binding197 – 1993ATP By similarity

Sites

Metal binding161Magnesium 2 By similarity
Metal binding521Magnesium 2 By similarity
Metal binding1071Magnesium 2 By similarity
Binding site411Substrate By similarity
Binding site521ATP By similarity
Binding site2041ATP By similarity

Experimental info

Sequence conflict521N → T in BAA03168. Ref.1
Sequence conflict821V → I in BAA03168. Ref.1
Sequence conflict1361V → W in BAA03168. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P46397 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 4CF38C48EC163047

FASTA22423,855
        10         20         30         40         50         60 
MPFLFVSGTG TGVGKTFSTA VLVRYLADQG HDVLPVKLVQ TGELPGEGDI FNIERLTGIA 

        70         80         90        100        110        120 
GEEFARFKDP LAPNLAARRE GVEPIQFDQI ISWLRGFDDP DRIIVVEGAG GLLVRLGEDF 

       130        140        150        160        170        180 
TLADVASALN APLVIVTSTG LGSLNAAELS VEAANRRGLT VLGVLGGSIP QNPDLATMLN 

       190        200        210        220 
LEEFERVTGV PFWGALPEGL SRVEGFVEKQ SFPALDAFKK PPAR

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization of the biotin biosynthetic genes of coryneform bacteria: cloning and sequencing of the bioA-bioD genes from Brevibacterium flavum."
Hatakeyama K., Hohama K., Vertes A.A., Kobayashi M., Kurusu Y., Yukawa H.
DNA Seq. 4:177-184(1993) [PubMed: 8161820] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MJ233.
[2]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D14083 Genomic DNA. Translation: BAA03168.1.
BA000036 Genomic DNA. Translation: BAB99998.1.
BX927155 Genomic DNA. Translation: CAF21267.1.
PIRI40337.
RefSeqNP_601806.1. NC_003450.3.
YP_226846.1. NC_006958.1.

3D structure databases

ProteinModelPortalP46397.
ModBaseSearch...

2D gel databases

World-2DPAGE0001:P46397.

Proteomic databases

PRIDEP46397.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1020552.
3344953.
GenomeReviewsGene locus Cgl2605 in contig BA000036_GR.
Gene locus cg2886 in contig BX927147_GR.
KEGGcgb:cg2886.
cgl:NCgl2516.
PATRIC21497256. VBICorGlu203724_2541.

Phylogenomic databases

HOGENOMHBG650065.
OMAAEAVGWC.
PhylomeDBP46397.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycCGLU196627:CG2886-MONOMER.

Family and domain databases

HAMAPMF_00336. BioD.
[Tree]
InterProIPR002586. CbiA_P_synth.
IPR004472. DTB_synth_BioD.
[Graphical view]
KOK01935.
PfamPF01656. CbiA. 1 hit.
[Graphical view]
PIRSFPIRSF006755. DTB_synth. 1 hit.
TIGRFAMsTIGR00347. BioD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBIOD_CORGL
AccessionPrimary (citable) accession number: P46397
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 11, 2002
Last modified: January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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