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Database: UniProt
Entry: A0A142LNH8_9PROT
LinkDB: A0A142LNH8_9PROT
Original site: A0A142LNH8_9PROT 
ID   A0A142LNH8_9PROT        Unreviewed;       661 AA.
AC   A0A142LNH8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AEM42_09600 {ECO:0000313|EMBL:AMS33774.1};
OS   Betaproteobacteria bacterium UKL13-2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS33774.1, ECO:0000313|Proteomes:UP000075227};
RN   [1] {ECO:0000313|Proteomes:UP000075227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Driscoll C.B.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP012157; AMS33774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142LNH8; -.
DR   STRING; 1690485.AEM42_09600; -.
DR   KEGG; beb:AEM42_09600; -.
DR   PATRIC; fig|1690485.4.peg.2189; -.
DR   Proteomes; UP000075227; Chromosome.
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   SMART; SM01209; GARS_A; 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; 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:UP000075227}.
FT   DOMAIN          1..452
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..320
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          583..660
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   661 AA;  71949 MW;  E0F514D48B8DF645 CRC64;
     MFNKILIANR GEIACRVIRT CKRLGIKTVA VYSDADRSAQ HVRLADEAYC IGGAPPRDSY
     LRADVILAVA QKAGAEAIHP GYGFLSENPH FARTCEAARI AFIGPTPDAI EKMGSKSAAK
     ALMEKAGVPV VPGYHGAEQD TAFLAEQSKK IGYPQLIKAV AGGGGKGMRL VERAEQFIAQ
     LDAAKREAKN AFGDDNVLIE RFIKGPHHIE FQVFGDSHGN VVHLFERECS IQRRHQKILE
     ETPSPFLDQV DDLMRDTMGA AAVAAARAID YRGAGTIEFI AGENREFFFM EMNTRLQVEH
     PITEMITGED LVEWQLLVAA GEALPLTQNE IITGGHAIEV RICAENPEND FLPEIGDLRV
     FVAPETAEDD DIRLDTGVVS GDHISIFYDP MIAKLITWGG DRPEAIRRMQ GALAETAVIG
     VKTNLAFLQT LVQHPAFLAG DTDTAFITKH NAALLQATSL SSAVLAAACA RVLADEATAA
     PQTDAWDSHT GWRLNQSASR LIEFKTMAGE EVACHVHETP HGLALTTPYA TTAFGWAINQ
     DGVFRIRLND QIQSAQVVRD RDALVVLTPS GRVSLSLFDP YHVEAVNASS EGRLTAMMPG
     RVVKLMVSVG DEVQKGQALI IMEAMKMEHT IISPRRGVIE HVAFQVGQMV PADAVLFSFN
     E
//
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