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Reviewed, UniProtKB/Swiss-Prot Q9JXF1 (BICOA_NEIMB)

Last modified November 3, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional enzyme birA/coaX
Including the following 2 domains:
    1- Recommended name:
            Biotin--[acetyl-CoA-carboxylase] synthetase
              EC=6.3.4.15
        Alternative name(s):
            Biotin--protein ligase
    2- Recommended name:
            Type III pantothenate kinase
              EC=2.7.1.33
        Alternative name(s):
            Pantothenic acid kinase
            PanK-III
Gene names
Name: birA/coaX
Ordered Locus Names: NMB2075
OrganismNeisseria meningitidis serogroup B [Complete proteome] [HAMAP]
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins By similarity.

Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis By similarity.

Catalytic activity

ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]. HAMAP MF_01274

ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. HAMAP MF_01274

Cofactor

Monovalent cations By similarity.

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. HAMAP MF_01274

Subcellular location

Cytoplasm Potential.

Sequence similarities

In the N-terminal section; belongs to the biotin--protein ligase family.

In the C-terminal section; belongs to the type III pantothenate kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional enzyme birA/coaX HAMAP MF_01274
PRO_0000270884

Regions

Nucleotide binding344 – 3518ATP By similarity
Region1 – 329329Biotin--protein ligase HAMAP MF_01274
Region336 – 592257Type III pantothenate kinase HAMAP MF_01274
Region433 – 4364Substrate binding By similarity

Sites

Active site4351Proton acceptor Potential
Binding site4261Substrate By similarity
Binding site4581ATP Potential
Binding site5081Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JXF1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9E27421DA2B41DE3

FASTA59264,701
        10         20         30         40         50         60 
MTVLKLSHWR VLAELADGLP QHVSQLARMA DMKPQQLNGF WQQMPAHIRG LLRQHDGYWR 

        70         80         90        100        110        120 
LVRPLAVFDA EGLRELGERS GFQTALKHEC ASSNDEILEL ARIAPDKAHK TICVTHLQSK 

       130        140        150        160        170        180 
GRGRQGRKWS HRLGECLMFS FGWVFDRPQY ELGSLSPVAA VACRRALSRL GLDVQIKWPN 

       190        200        210        220        230        240 
DLVVGRDKLG GILIETVRTG GKTVAVVGIG INFVLPKEVE NAASVQSLFQ TASRRGNADA 

       250        260        270        280        290        300 
AVLLETLLVE LDAVLLQYAR DGFAPFVAEY QAANRDHGKA VLLLRDGETV FEGTVKGVDG 

       310        320        330        340        350        360 
QGVLHLETAE GKQTVVSGEI SLRSDDRPVS VPKRRDSERF LLLDGGNSRL KWAWVENGTF 

       370        380        390        400        410        420 
ATVGSAPYRD LSPLGAEWAE KADGNVRIVG CAVCGEFKKA QVQEQLARKI EWLPSSAQAL 

       430        440        450        460        470        480 
GIRNHYRHPE EHGSDRWFNA LGSRRFSRNA CVVVSCGTAV TVDALTDDGH YLGGTIMPGF 

       490        500        510        520        530        540 
HLMKESLAVR TANLNRHAGK RYPFPTTTGN AVASGMMDAV CGSVMMMHGR LKEKTGAGKP 

       550        560        570        580        590 
VDVIITGGGA AKVAEALPPA FLAENTVRVA DNLVIYGLLN MIAAEGREYE HI 

« Hide

Cross-references

Sequence databases

AE002098 Genomic DNA. Translation: AAF42394.1.
PIRB81009.
RefSeqNP_275065.1.

3D structure databases

HSSPHSSP built from PDB template 1BIA based on UniProtKB P06709.
ModBaseSearch...

Genome annotation databases

GeneID903989.
GenomeReviewsGene locus NMB2075 in contig AE002098_GR.
KEGGnme:NMB2075.
NMPDRfig|122586.1.peg.1999.
TIGRNMB2075.

Phylogenomic databases

HOGENOMQ9JXF1.
OMAHECASSN.

Enzyme and pathway databases

BioCycNMEN122586:NMB_2075-MON.
BRENDA2.7.1.33. 293828.
6.3.4.15. 293828.

Family and domain databases

HAMAPMF_01274. Fused.
[Tree]
InterProIPR004619. Baf.
IPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
[Graphical view]
PANTHERPTHR12835. BirA_ligase. 1 hit.
PfamPF02237. BPL_C. 1 hit.
PF03099. BPL_LipA_LipB. 1 hit.
PF03309. Bvg_acc_factor. 1 hit.
[Graphical view]
TIGRFAMsTIGR00671. baf. 1 hit.
TIGR00121. birA_ligase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBICOA_NEIMB
AccessionPrimary (citable) accession number: Q9JXF1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents