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
//