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
//