ID A0A2I0C3I4_9PSED Unreviewed; 319 AA. AC A0A2I0C3I4; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 08-MAY-2019, entry version 8. 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 RT isolated 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 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: CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + CC H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, CC Rhea:RHEA-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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Complete proteome {ECO:0000313|Proteomes:UP000236285}; 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 BPL/LPL catalytic. {ECO:0000259|PROSITE: FT PS51733}. FT DNA_BIND 16 35 H-T-H motif. {ECO:0000256|HAMAP-Rule: FT MF_00978}. FT REGION 86 88 Biotin binding. {ECO:0000256|HAMAP-Rule: FT MF_00978}. FT REGION 114 116 Biotin binding. {ECO:0000256|HAMAP-Rule: FT MF_00978}. FT BINDING 110 110 Biotin. {ECO:0000256|HAMAP-Rule: FT MF_00978}. FT BINDING 181 181 Biotin. {ECO:0000256|HAMAP-Rule: FT 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 //