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Database: UniProt
Entry: A0A1Z8VD00_9PROT
LinkDB: A0A1Z8VD00_9PROT
Original site: A0A1Z8VD00_9PROT 
ID   A0A1Z8VD00_9PROT        Unreviewed;       329 AA.
AC   A0A1Z8VD00;
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=CBC21_07080 {ECO:0000313|EMBL:OUU57090.1};
OS   Proteobacteria bacterium TMED61.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1986601 {ECO:0000313|EMBL:OUU57090.1, ECO:0000313|Proteomes:UP000196561};
RN   [1] {ECO:0000313|EMBL:OUU57090.1, ECO:0000313|Proteomes:UP000196561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED61 {ECO:0000313|EMBL:OUU57090.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-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   -!- 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:OUU57090.1}.
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DR   EMBL; NHDO01000045; OUU57090.1; -; Genomic_DNA.
DR   Proteomes; UP000196561; 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   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
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   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:OUU57090.1}.
FT   DOMAIN          80..262
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   329 AA;  35699 MW;  4F5F3228810F9784 CRC64;
     MTADRTRLVR MLPTDRSLSL GELANATQID EATVAELLQQ LEQDGLPLHK ESDTHYRLLE
     PVLPIDVSDL VEQLENTGFA FARQAVVLDT VDSTSDWLSR EQQAGRDIHG KACITEFQSA
     GRGRRGRSWQ GSPYCHLMLS IGWRFQKEAA EMTGLSLSIG VAVAECLKEL AGVPVGLKWP
     NDLWYRDQKX GGILVDLNAS SGGATVAVVG IGINLHEPDS NQFDPGQPXT DLFSNAEGDL
     PPRTTIIGHV LGAIANVLDR FXQHQFAPDQ XRFNALDVFA GRXVRTESKG KRLEGVGAGA
     DELGRYCVHC ADGVVETINS GDISLSLAD
//
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