ID F0YHN6_AURAN Unreviewed; 1040 AA.
AC F0YHN6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN ORFNames=AURANDRAFT_66464 {ECO:0000313|EMBL:EGB05390.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB05390.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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; GL833142; EGB05390.1; -; Genomic_DNA.
DR RefSeq; XP_009040035.1; XM_009041787.1.
DR AlphaFoldDB; F0YHN6; -.
DR EnsemblProtists; EGB05390; EGB05390; AURANDRAFT_66464.
DR GeneID; 20225809; -.
DR KEGG; aaf:AURANDRAFT_66464; -.
DR eggNOG; KOG0238; Eukaryota.
DR eggNOG; KOG0540; Eukaryota.
DR InParanoid; F0YHN6; -.
DR OrthoDB; 1473822at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000002729; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
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; 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; 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; 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:UP000002729}.
FT DOMAIN 1..432
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 116..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 426..511
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 529..792
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 792..1026
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1040 AA; 107439 MW; 2652A13F6EC893D0 CRC64;
MKRLFIANRG EIAARIARTA RDRALPSVVA VAPEDEQLVA QYHCDATAPL RSAASYADSD
ELIAAALREG CDAVHPGYGF LSEDAAFSRN VRDAGLTFVG APTAALEVFG DKIAARRLAV
DAGVPVARGA VVGGAAELEA FLKDGIGAGV LKARAGGGGR GIRRVSLAGD LAADFERCAS
EASRSFGGAE EGLLVEDHVW SARHVEVQVA ADSCGAVATL FDRECSLQRR HQKLIEVAPA
PFLDDTLRRL IAEAAKALAA SSGLQGLGTF EFLINGDRFY FMECNPRLQV EHTVTEEIAG
VDLVAVQLAL DALRSRAAAP RGFSVQARVL AEKSGKPSCE PARKFNPPTN GVRVETALAE
GLGTHPSFDS LVAKVIVNAP TYERALDKAR RAVDDFGIEG PSTNLRFLSE LLSRPEVLDA
TATTTFVDDA FPDDEAAALG DDGDGALRSP TAGTVVSVAA VGEIARGKPV VVIEAMKMEH
VLAAPADGEV VAVRCAVGDV VSEGSVLAEV AIAAGAEAAA AEAAETVDLD APRPDLAALR
ARLALLDDAA RPEAVARRRK RGQLTAREHV AALCGESFKE LGGLAVAAQR RTRSEEELAA
KTPADGVLTG VGMVGAAPAV VVAVDATVLA GTQGFFHHHK LDRAVQVAAK RRLPIIALPE
GGGGRPNDGD VEGLMAAGLF ISTWHAYAAL AGVVPRVAVV SGYCFAGSAA IAGCSDVVIA
TETSSLGMGG PAMIEGGGLG RVKPEDVGPA PALAERGVVD VVAADDAAAL DAAKRYLSYF
AAPVAPPAPA GGDQRLLRQL VPENRKRAYD MRAILDVVCD EGSVFELRDR FGRSVITALA
RVDGRAVGIL ASDPARNGGA VDADAADKAA RFLRLCDAFG LPVVSLLDCP GFMVGPDAER
DGMVRKASRL FLAGAKLSVP VVAVVVRKAV GLGAMALCGG STKVPVDTLA FPTAEIGAMG
VEGAVNLGFK AKLDAVDGDE RAALFDKLCA AVHARGAATT AASQLEVDDV VDPAETRDRI
VAALAGYEPP PPKDGGLDAW
//
