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Database: UniProt
Entry: R5B871_9BACE
LinkDB: R5B871_9BACE
Original site: R5B871_9BACE 
ID   R5B871_9BACE            Unreviewed;       256 AA.
AC   R5B871;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Biotin--acetyl-CoA-carboxylase ligase {ECO:0000313|EMBL:CCX49042.1};
GN   ORFNames=BN813_02120 {ECO:0000313|EMBL:CCX49042.1};
OS   Bacteroides sp. CAG:927.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262753 {ECO:0000313|EMBL:CCX49042.1, ECO:0000313|Proteomes:UP000017907};
RN   [1] {ECO:0000313|EMBL:CCX49042.1, ECO:0000313|Proteomes:UP000017907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:927 {ECO:0000313|Proteomes:UP000017907};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCX49042.1}.
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DR   EMBL; CAWM010000084; CCX49042.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5B871; -.
DR   STRING; 1262753.BN813_02120; -.
DR   Proteomes; UP000017907; Unassembled WGS sequence.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
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; 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; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCX49042.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017907}.
FT   DOMAIN          1..188
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   256 AA;  28215 MW;  487E54A28D4AFD1E CRC64;
     MSNIISQPVI IRLPQGTSSN SILASKARDL PHGAVISLVE QTAGRGQRGN TWEAAPGMNL
     TLSMLLRPRN VKPNEQFMLS EMISLAIVRF LQTMLADTPH ASRIAIKWPN DIYVGDHKIC
     GILIEHSLSS AAITHTIAGI GININQVQFL SPAPNPISLA MLTGRTFDLH RAETLLAQNI
     LDLVNRYDNP ELFPELHALY INQLWRRKGA YKYMEAQSGR IFTASITDVL PTGHLQLTDT
     DGHTATYAFK EVAAVI
//
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