ID B4RC04_PHEZH Unreviewed; 246 AA.
AC B4RC04;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=biotin--[biotin carboxyl-carrier protein] ligase {ECO:0000256|ARBA:ARBA00024227};
DE EC=6.3.4.15 {ECO:0000256|ARBA:ARBA00024227};
GN OrderedLocusNames=PHZ_c1790 {ECO:0000313|EMBL:ACG78201.1};
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG78201.1, ECO:0000313|Proteomes:UP000001868};
RN [1] {ECO:0000313|EMBL:ACG78201.1, ECO:0000313|Proteomes:UP000001868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG78201.1,
RC ECO:0000313|Proteomes:UP000001868};
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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; CP000747; ACG78201.1; -; Genomic_DNA.
DR RefSeq; WP_012522343.1; NC_011144.1.
DR AlphaFoldDB; B4RC04; -.
DR STRING; 450851.PHZ_c1790; -.
DR KEGG; pzu:PHZ_c1790; -.
DR eggNOG; COG0340; Bacteria.
DR HOGENOM; CLU_051096_3_0_5; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000001868; 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 InterPro; IPR008988; Transcriptional_repressor_C.
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; SSF50037; C-terminal domain of transcriptional repressors; 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:ACG78201.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001868}.
FT DOMAIN 1..180
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 25793 MW; 2B66DE95A88D58E3 CRC64;
MAEHPPIEAY EALDSTNAEA RRRAEAGEAG PVWITAAVQT AGRGRRGRAW STRKGNLAAT
LLTVTDVPAA EAAQLSFVAA LAACDLADAC LGEGTARLKW PNDVLIHGRK AVGILVESGA
RPDGRLWLAV GIGVNLAHAP QDVERPAAAF AEYMAGPPPE PRAALEVLAA AFERWRRTWA
AGGFAPIAQA WTARAMGLGE RCEARLPGRT LAGVAEALDS DGALRLRLDD GSLERITAGD
VFFGGV
//
