ID A0A1G7CK87_9PROT Unreviewed; 668 AA.
AC A0A1G7CK87;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:SDE39729.1};
GN ORFNames=SAMN04488071_2839 {ECO:0000313|EMBL:SDE39729.1};
OS Kordiimonas lacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC Kordiimonadaceae; Kordiimonas.
OX NCBI_TaxID=637679 {ECO:0000313|EMBL:SDE39729.1, ECO:0000313|Proteomes:UP000183685};
RN [1] {ECO:0000313|EMBL:SDE39729.1, ECO:0000313|Proteomes:UP000183685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9109 {ECO:0000313|EMBL:SDE39729.1,
RC ECO:0000313|Proteomes:UP000183685};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNAK01000006; SDE39729.1; -; Genomic_DNA.
DR RefSeq; WP_068306710.1; NZ_LRUA01000006.1.
DR AlphaFoldDB; A0A1G7CK87; -.
DR STRING; 637679.GCA_001550055_03082; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000183685; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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:UP000183685}.
FT DOMAIN 4..458
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 597..666
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 668 AA; 71770 MW; 7E13981C6AC32B9F CRC64;
MSSRIKKLLI ANRGEIACRV MATCRQMGIK TVAVYSAADA HALHVKMADE AVFIGHAAAS
ESYLVGDKII DACKRTGADA VHPGYGFLSE NPEFAEACAK NGIIFVGPSA ASMRAMALKG
AAKQLMEEAG VPVVPGYHGE DQSVATLTAE AEKIGYPVLI KAVAGGGGKG MRKVFDAKEL
PAAIEAAARE GKNSFGNPEL LIEKYIQKPR HIEVQVFGDS DGHAVHLLER DCSLQRRHQK
VVEEAPAPGM SLEMRRAMGE AGVKAAEAIG YQGAGTVEFI VDVANGLESA PFYFMEMNTR
LQVEHPVTEM ITGQDLVEWQ IRIAEGKPLP LSQDEIEALA DGHAVEVRLY AEDPFNNFAP
AVGRIGMFDP FADTGPTGRI DAGVQAGDEV SIHYDPMIGK LIAWGEDREQ AIDALINLVA
ETPVTGLTTN RDFLLRALKH EDFRAGDVHT GFIEAFEDTL LAKPVTKAAD YATAAVAIIA
ARHVRAHDAD PWSLSDNFRL NLPASEKLWF DSGDGEFITA HVVEDRQNVS VTVGDDTFAY
KCPHLVDGIL TFSQDSLRQR LFVEVDAAHV SIVTDDRTLT VKRHARDGGA DDETDGPGTI
TAPMPGKILE VKVEDGASVE RGQPLLVMEA MKMEQTISAP RDGVVTGLSL KAGDQVADGA
TLLTISDE
//
