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A1U4A9 (BIOD_MARAV) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 31. 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:Maqu_2753
OrganismMarinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845)) [Complete proteome] [HAMAP]
Taxonomic identifier351348 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Marinobacter

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_00336

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
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 – 234234ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000302522

Regions

Nucleotide binding118 – 1214ATP By similarity
Nucleotide binding178 – 1792ATP By similarity
Nucleotide binding208 – 2103ATP By similarity

Sites

Metal binding181Magnesium 2 By similarity
Metal binding561Magnesium 2 By similarity
Metal binding1181Magnesium 2 By similarity
Binding site431Substrate By similarity
Binding site561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1U4A9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: AE738A58F84A20CC

FASTA23424,936
        10         20         30         40         50         60 
MAKHTFFVTG TDTGVGKTIV SAAILEAAKA AGKRTLAMKP IASGCDQTPE GLRNEDALML 

        70         80         90        100        110        120 
QAAITEKLPY DTINPIALEP AIAPHVAAQQ AGKQVTAQRI VGFCRGMQIR PADLLLIEGA 

       130        140        150        160        170        180 
GGWRVPLNDR ETYAAVPGEL KLPVILVVPL QLGCINHAML SAEAIRADGL VVAGWVGNHP 

       190        200        210        220        230 
EEQVMSCEQD TLNYLSTHLG APCLGVLPWL ENTDTAEMPA ILSRYLNITP LIEN

« Hide

References

[1]"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000514 Genomic DNA. Translation: ABM19828.1.
RefSeqYP_960015.1. NC_008740.1.

3D structure databases

ProteinModelPortalA1U4A9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1U4A9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4656015.
GenomeReviewsGene locus Maqu_2753 in contig CP000514_GR.
KEGGmaq:Maqu_2753.
PATRIC22460852. VBIMarAqu65105_3168.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0132.
HOGENOMHBG650065.
OMAANCVDPN.
PhylomeDBA1U4A9.
ProtClustDBCLSK719754.

Enzyme and pathway databases

BioCycMAQU351348:MAQU_2753-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_MARAV
AccessionPrimary (citable) accession number: A1U4A9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 31 of the entry and version 1 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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