ID A0A1I4YC02_9RHOB Unreviewed; 254 AA.
AC A0A1I4YC02;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=biotin--[biotin carboxyl-carrier protein] ligase {ECO:0000256|ARBA:ARBA00024227};
DE EC=6.3.4.15 {ECO:0000256|ARBA:ARBA00024227};
GN ORFNames=SAMN04487859_10191 {ECO:0000313|EMBL:SFN35526.1};
OS Roseovarius lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1005928 {ECO:0000313|EMBL:SFN35526.1, ECO:0000313|Proteomes:UP000198599};
RN [1] {ECO:0000313|EMBL:SFN35526.1, ECO:0000313|Proteomes:UP000198599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28463 {ECO:0000313|EMBL:SFN35526.1,
RC ECO:0000313|Proteomes:UP000198599};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOVP01000001; SFN35526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4YC02; -.
DR STRING; 1005928.SAMN04487859_10191; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000198599; Unassembled WGS sequence.
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 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:SFN35526.1}.
FT DOMAIN 1..192
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 254 AA; 26585 MW; EDBA5A1CF8A362C6 CRC64;
MKLGSEWDWP AGYGRRVLAS VDSTNAEAAR LAPGLAGPEW ILALEQTAGR GRRGRGWSDP
AGNFSASLVM RPNETPDRVA LRSFVASLAL YEALVAATGQ AEDFALKWPN DVLLKGGKLA
GILLESAGSG AGFSHFAIGI GVNLKEAPEV GAVEPGALRP VSVVSGTGVA IGPEAFLDLL
APAYARAEAQ FVTYGFEPIR HAWLARAARL GEVITARTSR EEVTGIFETV DGAGNLVLST
PTGRRAIAAA EVFF
//