ID Q5QW25_IDILO Unreviewed; 656 AA.
AC Q5QW25;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 24-JAN-2024, entry version 112.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:AAV81717.1};
GN OrderedLocusNames=IL0877 {ECO:0000313|EMBL:AAV81717.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV81717.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV81717.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AE017340; AAV81717.1; -; Genomic_DNA.
DR RefSeq; WP_011234128.1; NC_006512.1.
DR AlphaFoldDB; Q5QW25; -.
DR STRING; 283942.IL0877; -.
DR KEGG; ilo:IL0877; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_6; -.
DR OMA; LVKWQLM; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000001171; 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; 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:UP000001171}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 573..653
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 656 AA; 72445 MW; 1E137BE1CBAB6DEB CRC64;
MIKTLLIANR GEIACRIIAT AKKMGIRTVA VFSDADRNSR HVKLADQAVH IGPAASTDSY
LRADKIIAAA KQTDAEAIHP GYGFLSENED FADQCQANDI IFVGPPVSSI AAMGSKSAAK
SIMQDAGVPL VPGYHGSEQD IKTLKAEAEK VGFPLLLKAA YGGGGKGMRV VENMGEFDDA
LNSAKREAKS SFGNDKMLME RFIRNPRHVE IQVFTDEHGN AVYLAERDCS VQRRHQKVLE
EAPAPALTEK TRTEMGEAAI RAAQAINYVG AGTVEFLFDQ SGEFYFMEMN TRLQVEHPVT
EMITGQDLVE WQLLVASGQP LPLAQNDIQV NGHAFEARIY AEDPDNDFLP CTGTIKHLRT
PAEENGIRID TGIEEGDEIS AFYDPMIAKL IVWDTDRTRA LLRLQKALRE YRLTGLTTNV
DFLHRLASHP EFVKTNLTTE FIQQHQEELL PDSSVNCQQI ATEAALFDIC QRQQQRGSSP
WQSGNAFRMN SAATHTVPLQ FGEETYSISL IETANGEFLQ QVDDESIQWQ ASLTDDKLTL
TAGSMRYHRY VSADDQQITV FTDNGPMTFH RHRVTDTLSD EAAHGGHVAP MNGTIMEVLV
KKGDTVKKDQ PLVIMEAMKM EYTIKAGHEG EVTDVFFAAG DLVSDGDELL TVSEAE
//