ID A0A1E4SF71_9ASCO Unreviewed; 2218 AA.
AC A0A1E4SF71;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acetyl-coenzyme-A carboxylase {ECO:0000313|EMBL:ODV78179.1};
GN ORFNames=CANTADRAFT_54402 {ECO:0000313|EMBL:ODV78179.1};
OS Suhomyces tanzawaensis NRRL Y-17324.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Suhomyces.
OX NCBI_TaxID=984487 {ECO:0000313|EMBL:ODV78179.1, ECO:0000313|Proteomes:UP000094285};
RN [1] {ECO:0000313|Proteomes:UP000094285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17324 {ECO:0000313|Proteomes:UP000094285};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000861};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001455};
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; KV453914; ODV78179.1; -; Genomic_DNA.
DR RefSeq; XP_020063301.1; XM_020210320.1.
DR STRING; 984487.A0A1E4SF71; -.
DR GeneID; 30984456; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000094285; 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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR049074; ACCA_BT.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF21385; ACCA_BT; 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; PS00188; BIOTIN; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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:UP000094285}.
FT DOMAIN 46..555
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 204..396
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 682..756
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1473..1808
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1812..2127
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 428..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2157..2184
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2218 AA; 248056 MW; EEE9CCD86C1453E0 CRC64;
MSESPDKDYS QLHAGLAPHF KGLNSVHRAE PGKITDFVKS HQGHTVISKV LIANNGIAAV
KEIRSVRKWA YETFGDERAV QFTVMATPED LEANAEYIRM ADQFVEVPGG TNNNNYANVD
LIIEIAERTN VHAVWAGWGH ASENPLLPEG LAASPNKIIF IGPPGSAMRS LGDKISSTIV
AQHAQVPCIP WSGTGVDQVT VDPETNLVSV EDEIYQQGCC TSPEDGLVKA RQIGYPVMIK
ASEGGGGKGI RRVDDEKDFI ALYKQAANEI PGSPIFIMKL AGSARHLEVQ LLADQYGTNI
SLFGRDCSVQ RRHQKIIEEA PVTIANKDTF HQMENAAVRL GRLVGYVSAG TVEYLYSHAD
DKFYFLELNP RLQVEHPTTE MVTGVNLPAA QLQIAMGIPM HRIRDIRTMY GVDPHTATPI
DFEFTNEDSL TSQRRPVPKG HTTACRITSE DPGEGFKPSG GNLHELNFRS SSNVWGYFSV
GTKSSIHSFS DSQFGHIFAF GENRQASRKH MVVALKELSI RGDFRTTVEY LIKLLETPAF
EGNTITTGWL DELISKKLTA ERPDPIIATV CGAVTKAHIQ SEEDKKLYIQ TLEKGQVPNN
SLLRTVFPVE FIYEGQRYKF TATKSSNDSY TLFLNGTRCV VGVRPLSDGG LLCAIGGKSH
SVYWKEEASA TRLSVDSKTC LLEVENDPTQ LRTPSPGKLV KYLVESGEHV TAGQAYAEVE
VMKMVMPLIA QENGVVQVIK QPGSTVNAGD ILAILSLDDP SKVKHALPYE GTLPELGEPI
VLGTKIVHKF FLYSSILRNI LTGYDNQVIM NSTLKSLIEV LKSKDLPFSE WNLQASALHS
RLPIKLDESL NALVQRATSR GADFPARQIL KLIQKTATDP ETDASFEAVA APLVEIATRY
SNGLVEHEFD FFAKLIMEYY DIETLFSGET TREDDVILKL RDENKSDLNK VTTICLSHSR
VSAKNNLLLA IMEEYQPVLQ SSSSIAVSIR QALKSIVTLD ARGTAKVALK AREILIQCSL
PSIQERSDQL EHILRSAVLQ TSYGEIYAKH REPRLDIIQE VVDSKHTVFD VLPQFLVNND
EWVSIAASEV YIRRSYRAYS LGPVSYHFHD RLPILEWKFQ LPSLTSAQYN SIQHLKNEQN
KMDRAASVSD LSFVVDTSTE QKTRTGILVP CRHLDDVDEM IAAALERFQP SDAITFEAKG
EQPAFTNVFN VVITNHDSYT TEEEVLAKIQ EVIDDFKDDF KAVAIRRITF VVANKVGVYP
KYFTFNAPDY IENKVIRHIE PALAFQLELG RLDNFDIKPI FTDNRNIHVY EALGKNARSD
KRFFTRGIVR TGILRDEISI SEYLIAESNR LMSNILDALE IIDTSNSDLN HIFINFSNVF
NVLPEEVEAA FGSFLERFGR RLWRLRVTGA EIRIVCTDPT TGNSFPLRAI INNVSGYVVK
SELYMEVKNT KGEWVFKSMG QPGSMHYRPI STPYPAKESL QPKRYRAHNM GTTYVYDFPE
LFRQATLSQW KKHPKLKVPK DVFTSFELIN DENEDLIAVE REPGANKIGM VGFKVVAKTP
EYPRGRQMII VANDITHKIG SFGPEEDKYF NQCTELAREL GIPRIYLSAN SGARIGIADE
LVPLFKVAWN EDGVPEKGFK YLYLTPEDMK AITDSGKGHT VVAERSVEEG QERYVIKSIV
GAEDGLGVEC LKGSGLIAGA TSRAYKDIFT ITLVTCRSVG IGAYLVRLGQ RAIQIEGQPI
ILTGAPAINK LLGREVYSSN LQLGGTQIMY RNGVSHLTAT DDLAGVEKIL EWLSFVPAKR
GMPVPTLPSE DTWDRDIDYY PPKDEPFDVR WMIEGREIDG DFETGLFDKG SFQETLSGWA
KGVVVGRARL GGIPIGIIGV ENRMVENLIP ADPANPDSTE VMIQEAGQVW YPNSAFKTAQ
AIRDFNNGEQ LPLMILANWR GFSGGQKDMY NEVLKYGAFI VDALTEFKQP IFTYIPPNGE
LRGGSWVVVD PTINAEMMEM YADVDSRAGV LEPEGMVGIK YRRDKLLSTM QRLDPTYAEL
KSKLADASLS AEEHSQISAK VTAREKMLLP IYAQISVQFA DLHDRSGRML AKGVIRQEIK
WVDARRVFFW RLRRRLNEEY LLKLIGEQLK SPTKLEKVAR LKSWMPAVDY EDDEAVSTWI
EENHSKLQNN IEELKQEAIR QKIHSFVNED PNQSASVVKE IFGTLSEEQK SELLKSLQ
//
