ID A0A010RJ13_PSEFL Unreviewed; 653 AA.
AC A0A010RJ13;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:EXF92661.1};
GN ORFNames=HK44_010950 {ECO:0000313|EMBL:EXF92661.1};
OS Pseudomonas fluorescens HK44.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF92661.1, ECO:0000313|Proteomes:UP000022611};
RN [1] {ECO:0000313|EMBL:EXF92661.1, ECO:0000313|Proteomes:UP000022611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK44 {ECO:0000313|EMBL:EXF92661.1,
RC ECO:0000313|Proteomes:UP000022611};
RX PubMed=21742869; DOI=10.1128/JB.05530-11;
RA Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA Karpinets T.V., Brown S.D., Sayler G.S.;
RT "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT HK44.";
RL J. Bacteriol. 193:5009-5010(2011).
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:EXF92661.1}.
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DR EMBL; AFOY02000016; EXF92661.1; -; Genomic_DNA.
DR RefSeq; WP_019692880.1; NZ_AFOY02000016.1.
DR AlphaFoldDB; A0A010RJ13; -.
DR PATRIC; fig|1042209.11.peg.4595; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000022611; 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; 3.30.470.20; 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:UP000022611}.
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 577..653
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 653 AA; 71141 MW; 17D0278D9F48390A CRC64;
MPTLRKILIA NRGEIACRIQ RTAQALGYRT VAVFSDADAD ALHVQMADEA VNIGPAAVAQ
SYLNSAAIID AALRSGADAI HPGYGFLSEN AEFATACAQA GITFIGPSPA AIELMGSKRL
SKIAMLAAGV PCINGYQGAE QDDATLSREA ERIGYPLMIK ASAGGGGRGM RLVHSADKLL
EQIRTARSEA LHAFGSDELI LEQALIEPRH IEIQLFGDQH GNLIYLGERD CSIQRRHQKV
IEEAPCPVMT AELRQAMGDA ALKAGRAVNY VGAGTVEFLL DARGQFYFLE MNTRLQVEHP
VTELITGLDL VAWQLDVAAG LSLALRQEQV ELKGHAMEAR LYAEDPAQGF LPQTGRITRW
EPALADGVRI DHGLLEDQQV SPFYDPLLGK IIAYGATREE ARRKLLRAVQ DSALLGLQTN
QRLLAGLLEH PQFIARDFNT GFIAQHFADH PSLHPHAPTA EELAIATALF YQQSAGAHPP
RLAGWRNNAN VPLLQQIGLN GDRWSTEVSV LPDRQLRIQV AGETLQLKLL DINERWANLE
INGIRRRYAW QLTAGQLWLF TRPGSLLLQD QTLAPVSGQV GTRTGTLKAP MDGAIVDVLI
SEGSSVSKGQ LLLVLEAMKM EHPLKAGIDG VIKRLQVSLG DQVKNRQILL EVE
//
