(data stored in SCRATCH zone)

SWISSPROT: C5BCC2_EDWI9

ID   C5BCC2_EDWI9            Unreviewed;       319 AA.
AC   C5BCC2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin operon repressor {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000256|HAMAP-Rule:MF_00978};
DE            EC=6.3.4.15 {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin--protein ligase {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000256|HAMAP-Rule:MF_00978};
GN   Name=birA {ECO:0000256|HAMAP-Rule:MF_00978};
GN   OrderedLocusNames=NT01EI_0161 {ECO:0000313|EMBL:ACR67413.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67413.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase
CC       and a biotin-operon repressor. In the presence of ATP, BirA
CC       activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-
CC       5'-AMP or holoBirA) complex. HoloBirA can either transfer the
CC       biotinyl moiety to the biotin carboxyl carrier protein (BCCP)
CC       subunit of acetyl-CoA carboxylase, or bind to the biotin operator
CC       site and inhibit transcription of the operon. {ECO:0000256|HAMAP-
CC       Rule:MF_00978}.
CC   -!- CATALYTIC ACTIVITY: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide
CC       ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-
CC       dioxide ligase (ADP-forming)]. {ECO:0000256|HAMAP-Rule:MF_00978}.
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00978}.
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DR   EMBL; CP001600; ACR67413.1; -; Genomic_DNA.
DR   RefSeq; WP_015869628.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0161; -.
DR   EnsemblBacteria; ACR67413; ACR67413; NT01EI_0161.
DR   GeneID; 7958758; -.
DR   KEGG; eic:NT01EI_0161; -.
DR   PATRIC; fig|634503.3.peg.148; -.
DR   eggNOG; ENOG4105HJX; Bacteria.
DR   eggNOG; COG0340; LUCA.
DR   eggNOG; COG1654; LUCA.
DR   HOGENOM; HOG000041812; -.
DR   KO; K03524; -.
DR   OMA; RAAVWKH; -.
DR   OrthoDB; POG091H01NJ; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009305; P:protein biotinylation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00978; Bifunct_BirA; 1.
DR   InterPro; IPR030855; Bifunct_BirA.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR004409; Biotin_operon_repress_HTH.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   PANTHER; PTHR12835:SF10; PTHR12835:SF10; 1.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF50037; SSF50037; 1.
DR   TIGRFAMs; TIGR00121; birA_ligase; 1.
DR   TIGRFAMs; TIGR00122; birA_repr_reg; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BCC2.
DR   SWISS-2DPAGE; C5BCC2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Biotin {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00978, ECO:0000313|EMBL:ACR67413.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Repressor {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00978}.
FT   DOMAIN       66    254       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
FT   DNA_BIND     22     41       H-T-H motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   REGION       89     91       Biotin binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   REGION      116    118       Biotin binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   BINDING     112    112       Biotin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   BINDING     183    183       Biotin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
SQ   SEQUENCE   319 AA;  34687 MW;  FAA90E1F7455FFE5 CRC64;
     MKDITVPLKL ISQLADGDFH SGEHLGESLG MSRAGINKHI QTLRDWGIDV FTVPGKGYCL
     PTPMQLLNTE TIGALLPQGR VTVLPVVDST NQYLLERIGE LASGDACVAE YQQAGRGRRG
     RHWFSPFGAN LYLSMYWRLE QGPAAAMGLS LVIGIVMAEV LQALGAAGVK VKWPNDLYLN
     DRKLAGILVE LTGKTGDAAN IVVGAGINLM MRNPDTSVVD QQWINLQEAG VNIDRNQLVA
     CLLSRLRSTL ADFEVRGLSP FISRWRVLDN FVDRPVRLII GEQVIHGIAR GIDAQGALLL
     ERDGVITPFI GGEISLRAG
//

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