ID A0A2I0C3I4_9PSED Unreviewed; 319 AA. AC A0A2I0C3I4; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 11-DEC-2019, entry version 9. 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 ORFNames=CW309_31905 {ECO:0000313|EMBL:PKF22597.1}; OS Pseudomonas hunanensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1247546 {ECO:0000313|EMBL:PKF22597.1, ECO:0000313|Proteomes:UP000236285}; RN [1] {ECO:0000313|EMBL:PKF22597.1, ECO:0000313|Proteomes:UP000236285} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P11 {ECO:0000313|EMBL:PKF22597.1, RC ECO:0000313|Proteomes:UP000236285}; RA Pan J.; RT "High quality draft genome sequence of Pseudomonas hunanensis P11 isolated RT from the high-arsenic soil."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a CC biotin-operon repressor. In the presence of ATP, BirA activates biotin CC to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) CC complex. HoloBirA can either transfer the biotinyl moiety to the biotin CC carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or CC bind to the biotin operator site and inhibit transcription of the CC operon. {ECO:0000256|HAMAP-Rule:MF_00978}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + CC N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; CC EC=6.3.4.15; Evidence={ECO:0000256|HAMAP-Rule:MF_00978}; CC -!- SIMILARITY: Belongs to the biotin--protein ligase family. CC {ECO:0000256|HAMAP-Rule:MF_00978}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PKF22597.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PISL01000107; PKF22597.1; -; Genomic_DNA. DR RefSeq; WP_004575794.1; NZ_PISL01000107.1. DR Proteomes; UP000236285; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0009305; P:protein biotinylation; IEA:UniProtKB-UniRule. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule. DR CDD; cd16442; BPL; 1. 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; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR013196; HTH_11. DR InterPro; IPR008988; Transcriptional_repressor_C. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. 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 PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00978}; KW Biotin {ECO:0000256|HAMAP-Rule:MF_00978}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00978}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00978, ECO:0000313|EMBL:PKF22597.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00978}; 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 73..251 FT /note="BPL/LPL catalytic" FT /evidence="ECO:0000259|PROSITE:PS51733" FT DNA_BIND 16..35 FT /note="H-T-H motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978" FT REGION 86..88 FT /note="Biotin binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978" FT REGION 114..116 FT /note="Biotin binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978" FT BINDING 110 FT /note="Biotin" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978" FT BINDING 181 FT /note="Biotin" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978" SQ SEQUENCE 319 AA; 35086 MW; E3E97998C6C7433C CRC64; MLKLLNLLKD GRFHSGEALG AALGVSRSAV WKQLQHLESE LNLTIHKVRG RGYQLAAPLA LLEAQAIAEF AVGEQWPVFI HETIDSTNAE GLRLASEGQA APFLVLAERQ SAGRGRRGRQ WVSPFAENLY YSLVLRVDGG MRQLEGLSLV VGLAVMRTLQ AFGVKDVGLK WPNDVLVRGQ KITGILLELV GDPADVCHVV LGIGVNVNMQ VNEQVDQQWT SMRREVGAAI DRNHLVALLS QHLQHELARH RRYGFAAFQE EWEQAHLWQG RNVSLVAGST RIDGVVLGVD GQGGLRLEVD GMEKSFSGGE LSLRLRDDS //