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Database: UniProt
Entry: Q5QW25_IDILO
LinkDB: Q5QW25_IDILO
Original site: Q5QW25_IDILO 
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
//
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