Bifunctional enzyme BirA/CoaX - Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)

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Q9JWI7 (BICOA_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional enzyme BirA/CoaX

Including the following 2 domains:

Biotin--[acetyl-CoA-carboxylase] synthetase
EC=6.3.4.15
Alternative name(s):
Biotin--protein ligase
Type III pantothenate kinase
EC=2.7.1.33
Alternative name(s):
PanK-III
Pantothenic acid kinase

Gene names

Name:	birA/coaX
Ordered Locus Names:	NMA0357

Organism

Neisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]

Taxonomic identifier

122587 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins By similarity. HAMAP-Rule MF_01274 Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis By similarity. HAMAP-Rule MF_01274
Catalytic activity	ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]. HAMAP-Rule MF_01274 ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. HAMAP-Rule MF_01274
Cofactor	Monovalent cations By similarity.
Pathway	Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. HAMAP-Rule MF_01274
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_01274.
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.

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Kinase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from electronic annotation. Source: InterPro coenzyme A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin-[acetyl-CoA-carboxylase] ligase activity Inferred from electronic annotation. Source: EC pantothenate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 592

592

Bifunctional enzyme BirA/CoaX HAMAP-Rule MF_01274

PRO_0000270883

Regions

Nucleotide binding

344 – 351

ATP By similarity

Region

1 – 329

329

Biotin--protein ligase HAMAP-Rule MF_01274

Region

336 – 592

257

Type III pantothenate kinase HAMAP-Rule MF_01274

Region

433 – 436

Substrate binding By similarity

Sites

Active site

435

Proton acceptor Potential

Binding site

426

Substrate By similarity

Binding site

458

ATP Potential

Binding site

508

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JWI7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7ED2E0CD3B31C630
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FASTA

592

64,469

        10         20         30         40         50         60 
MTVLKPSHWR 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 GLKTQIKWPN 

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

       250        260        270        280        290        300 
AVLLETLLAE 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 KVDGNVRIVG 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 DNLVIHGLLN LIAAEGGESE HT

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References

[1]

"Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491."
Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S.

Barrell B.G.
Nature 404:502-506(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Z2491.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL157959 Genomic DNA. Translation: CAM07655.1.
PIR	H82031.
RefSeq	YP_002341868.1. NC_003116.1.
3D structure databases
HSSP	HSSP built from PDB template 1BIA based on UniProtKB P06709.
ProteinModelPortal	Q9JWI7.
ModBase	Search...
Protein-protein interaction databases
STRING	122587.NMA0357.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAM07655; CAM07655; NMA0357.
GeneID	906361.
KEGG	nma:NMA0357.
PATRIC	20361386. VBINeiMen132687_0415.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0340.
HOGENOM	HOG000220772.
KO	K01947.
OMA	EGGESEH.
ProtClustDB	PRK13325.
Enzyme and pathway databases
BioCyc	NMEN122587:GI3Q-356-MONOMER.
UniPathway	UPA00241; UER00352.
Family and domain databases
HAMAP	MF_01274. Pantothen_kinase_3. Fused.
InterPro	IPR004408. Biotin_CoA_COase_ligase. IPR003142. BPL_C. IPR004143. BPL_LipA_LipB. IPR008988. Transcriptional_repressor_C. IPR004619. Type_III_PanK. [Graphical view]
PANTHER	PTHR12835. PTHR12835. 1 hit.
Pfam	PF02237. BPL_C. 1 hit. PF03099. BPL_LplA_LipB. 1 hit. PF03309. Pan_kinase. 1 hit. [Graphical view]
SUPFAM	SSF50037. Transcr_rep_C. 1 hit.
TIGRFAMs	TIGR00671. baf. 1 hit. TIGR00121. birA_ligase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BICOA_NEIMA

Accession

Primary (citable) accession number: Q9JWI7
Secondary accession number(s): A1IPI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents