ID G4E4Y8_9GAMM Unreviewed; 273 AA.
AC G4E4Y8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=ThisiDRAFT_1367 {ECO:0000313|EMBL:EGZ46743.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ46743.1};
RN [1] {ECO:0000313|EMBL:EGZ46743.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ46743.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) 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 -!- 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:EGZ46743.1}.
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; AGFD01000023; EGZ46743.1; -; Genomic_DNA.
DR AlphaFoldDB; G4E4Y8; -.
DR STRING; 765914.ThisiDRAFT_1367; -.
DR eggNOG; COG0340; Bacteria.
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:EGZ46743.1}.
FT DOMAIN 18..201
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 273 AA; 29000 MW; 6B668600F527956F CRC64;
MLSAERVFAA LPERLQHSLP KPLVLASVDS THAMLLGQAR SKKHITCQIC LAEYQTAGRG
RRGSCWVMPA GSGIALSLLW PVDASSALAP TLSLAFGVVI AEALERLAPS PTAHIGLKWP
NDLLVEGQKL GGLISEAVFC GGQPRALVVS VGLNVCLPAD APIDQAWTDL VRTGLQPPKP
SRSVIAAVLI TALVDVLDTY PAHGFAAYAP RWQARDVSHG RAVSFIQAGQ TMQGIAQGLD
LEGNLRVLCQ GQTYTLRSAE CSLRIATDTP SRR
//
