ID A0A0B3C4B2_9PSED Unreviewed; 662 AA.
AC A0A0B3C4B2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KHO66367.1};
GN ORFNames=PT85_01990 {ECO:0000313|EMBL:KHO66367.1};
OS Pseudomonas flexibilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO66367.1, ECO:0000313|Proteomes:UP000030980};
RN [1] {ECO:0000313|EMBL:KHO66367.1, ECO:0000313|Proteomes:UP000030980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO66367.1,
RC ECO:0000313|Proteomes:UP000030980};
RA Shin S.-K., Yi H.;
RT "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KHO66367.1}.
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DR EMBL; JTAK01000001; KHO66367.1; -; Genomic_DNA.
DR RefSeq; WP_039605779.1; NZ_JTAK01000001.1.
DR AlphaFoldDB; A0A0B3C4B2; -.
DR STRING; 706570.PT85_01990; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000030980; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000030980}.
FT DOMAIN 3..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 589..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 662 AA; 71640 MW; BCE7B4C32E9D91E8 CRC64;
MPAFNKILIA NRGEIACRVM RTAHELGYRT VAVYSEADAN ARHVQLADEA VCIGPAQVNQ
SYLVIDNIIA AAKKTGADAI HPGYGFLSEN ADFARACEAA GIVFIGPTVK AIHLMGSKRL
SKIAMLEASV PCIPGYEGAA QDDETLIREA ERIGYPLMIK ASAGGGGRGM RLVHEAGQLQ
EQIRTARSEA QNAFGSGELI LERAVIRPRH VEIQVFGDQH GNIVYLGERD CSVQRRHQKV
VEEAPCPVMT PELRKAMGEA AVKAAASVNY VGAGTVEFLL DASGEFFFLE MNTRLQVEHP
VTELITGQDL VAWQIRAAEG QPLPLKQEEI QLTGHAIEVR LYAEDAAHNF LPQTGKVLRW
EPELLDGVRI DHGLVEGQDV TPFYDPMLAK VIAYGATRAD ALRKLIRAVE NCVLLGVNGN
QRFLANLLNH PEFAAGKATT AFIAEHFSND ESLTPQAPAA RELAVAAALL YQASANGRAH
QQQLAGWRSA GSAPWQFTLK QGEQSHKVAL QVQRDGTQPA LLASVGDSQL SLRLLHSDGR
WLTFELDGIR QRQAYHLDGE NLWLYGHFGN LALTDVSHAP AGGQSAASSG TIKAPMDGAI
VDVLVGEGVR VTKGQLLVVL EAMKMEHPLK AGIDGVIRRV GASRGDQVKN RQVLVEIEAE
EA
//
