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Database: UniProt
Entry: A8WMY1_CAEBR
LinkDB: A8WMY1_CAEBR
Original site: A8WMY1_CAEBR 
ID   A8WMY1_CAEBR            Unreviewed;      1665 AA.
AC   A8WMY1;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN   ORFNames=CBG00376 {ECO:0000313|EMBL:CAP21836.2,
GN   ECO:0000313|WormBase:CBG00376}, CBG_00376
GN   {ECO:0000313|EMBL:CAP21836.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP21836.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP21836.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP21836.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR   EMBL; HE600968; CAP21836.2; -; Genomic_DNA.
DR   STRING; 6238.A8WMY1; -.
DR   WormBase; CBG00376; CBP46648; WBGene00023773; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_2_1; -.
DR   InParanoid; A8WMY1; -.
DR   OMA; EEPILRH; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 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   Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45728:SF2; ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000008549}.
FT   DOMAIN          27..513
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          179..373
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          642..717
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          992..1316
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1319..1603
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   1665 AA;  187801 MW;  876B737371651464 CRC64;
     MSDLGEENSS DPDRIEEFVR QFVGGKSIKR VLIANNGLAA MKCLISIRQW LQNQFVTSDV
     VSFVCIATED EMKSASHYLK LADEIVMAPA GSNSKNFANV EVITSLALKS RVDAVYVGWG
     HASENPELAR RLRKNDIIFI GPSEKSIVAS GDKIISTIIA QSIGMPTVTW SGRDVKVEKC
     VDFEHFHELR AQATIKSAKE GLEAIEKYGI GVPMMIKASE GGGGKGIRKC EKMEDFERLF
     KEVEIEVPNS PIFLMKCMEG ARHVEIQIIG DKHGEVIALS SRDCTIQRRC QKVIEEAPAS
     IVPEEIMKNM KKDAIAFANF VDYYSAGTVE LLFVPSTNQY FFLELNPRLQ VEHPCTESVC
     DVNVPALQFQ IAMGRKLTDI PCVRRFKERE ERGENSKMHC FAARVTCEDP NDRFLPSTGT
     VRSLKFNSTS KAWAYFSLTD GSTVHEFADS QIGHVFARGR DRSEAITNLK HALHNLKIDA
     TFPTQSDYLI DLLSLEKFKS NQYDTQWLDQ RIAKREQQKL TLPIDHLIAI SAAAIGRSKI
     RSIFERYENN LRTGKIVLPV ELSRSTEVEL EINNVKYFLN VFEETPLKYH LRLGTQETTV
     EMLKYGTHNL AIHQGKSTDY VLEETEEVYL IKIGGNKLKF SKMDTNDASC LRSPYTGKFL
     EYKVQPGEFV QVGQTYAQIE SMKMVFDVVT KVAPGRLIPI AKDGDLINPG SILGRLEIDK
     HIQDQLMTSE KFDGKMTGWK VEEKSDFEKA QLILEGRGAM DYQINQLVSG LVNSNATQLI
     DRFIELAEPF DSRDGFDESV QRLLQEESPV FEQIVDLIHS NTNQKTKEKL IMGILETIQN
     PQEYEESLMA LYKTCLLRNF KSMAAMVAKI LKPESSEPLE IKKSQNLGSM RFRNTQKEYS
     SFQLTNAVFV ALLEFTACSS GIKNTNFVAN RIDISIDISR EQAEEVLEIN ERFLKAAGVT
     EILLTSSSET LWFSWKVDRF HLEVLSSTES PEFLPPNPRD FKRSLASLNR TTYIYDFPYL
     FASIGNLEYQ ELIVDEKTHQ LQMISDTEEL ERRAVGGLNT CSVVAWLMKL EIEQNDQREF
     VLIGNDVTHQ VGSFAQPEHE LFELASRLAR ERKIPRINIS CNSGARIGLA RDVLDVLKVK
     LKPNGHDFDY LYVDSSEKER IGNQIVYKEQ GEELKLVAVK GKKVRHKVGG NEYIGVENLM
     GSGAIGGETS RAYREIPTYC YVTGRSVGIG AYTARLARRI IQHKDSHLIL TGATALNTLL
     GKKVYASNNR LGGVEIMSNN GIAHATVSSD VEGVEKLVQW LKYLPVKQKE YPFFKCLDKE
     DVKVEDVKVN KDEMQLDVRN IIEGFDGKQG IFDFGSFDEI CTSWAASIVT GRAKLNGLPV
     GVIGSQWKSY EKQQLADESV EKSEEVTVTR AGQVWYPESA FKTSQAISDF NRESLPLVMI
     ASLRGFSGGR KDMSDQVLTF GAHIIDELSQ YQQPVIVYIP AGGELRGGAW AVVDSNINRG
     IVHVIADETC RGGILEPNAV VGIKIREAQI GKIMERSGVV SVDVEDSVKS AFKKACVDFA
     DMHDRWPRME YVGAIRQVTS LQNTRAVFWK ILKKELILVE IADRYSNAPI YPKPTHSEAL
     EWVKKRTEEE EDLRKYYTDV FCEDVSREIQ KSKNRFEEAC ATWQL
//
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