ID A0A222E6C9_9RHOB Unreviewed; 247 AA.
AC A0A222E6C9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=biotin--[biotin carboxyl-carrier protein] ligase {ECO:0000256|ARBA:ARBA00024227};
DE EC=6.3.4.15 {ECO:0000256|ARBA:ARBA00024227};
GN Name=birA {ECO:0000313|EMBL:ASP21757.1};
GN ORFNames=ANTHELSMS3_03105 {ECO:0000313|EMBL:ASP21757.1};
OS Antarctobacter heliothermus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Antarctobacter.
OX NCBI_TaxID=74033 {ECO:0000313|EMBL:ASP21757.1, ECO:0000313|Proteomes:UP000203589};
RN [1] {ECO:0000313|EMBL:ASP21757.1, ECO:0000313|Proteomes:UP000203589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS3 {ECO:0000313|EMBL:ASP21757.1,
RC ECO:0000313|Proteomes:UP000203589};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Antarctobacter heliothermus Strain SMS3 Isolated from a
RT culture of the Diatom Skeletonema marinoi.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000933};
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; CP022540; ASP21757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222E6C9; -.
DR KEGG; aht:ANTHELSMS3_03105; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000203589; Chromosome.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR NCBIfam; TIGR00121; birA_ligase; 1.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ASP21757.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000203589}.
FT DOMAIN 6..184
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 247 AA; 26188 MW; 8AF6688375D6E868 CRC64;
MDWPQGYGRR VLAEVDSTNA EAVRVAGTLA GPEWILGLQQ TAARGRRGRA WVNPAGNFAA
TLVMRPTETP DRVALRSFVA ALALYDALER VTGTAIGLSL KWPNDVLLNG GKLAGILLES
IGGPGGHLAI GIGVNLLAAP EMSQVEERAV TPVALLPETG VRVTPEAFLS ALASAYATHE
ARFVTYGFEP IRSLWLQRAA RLGETITART ARDTETGVFE TVDATGQLVL KTPKGRVTVA
AADIFFG
//