ID M7SLD9_EUTLA Unreviewed; 2268 AA.
AC M7SLD9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Putative acetyl-carboxylase protein {ECO:0000313|EMBL:EMR67184.1};
GN ORFNames=UCREL1_5819 {ECO:0000313|EMBL:EMR67184.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR67184.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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; KB706494; EMR67184.1; -; Genomic_DNA.
DR RefSeq; XP_007793722.1; XM_007795531.1.
DR STRING; 1287681.M7SLD9; -.
DR KEGG; ela:UCREL1_5819; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000012174; 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 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:UP000012174}.
FT DOMAIN 64..572
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 221..413
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 699..773
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1514..1852
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1856..2171
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2268 AA; 253103 MW; B27BE9564AE60580 CRC64;
MSQSNGHGAA NGVNSNRTVP VTNGKASYAE KHRIPEHYIG GNKLQNAAPS KVKDFVAAHD
GHTVITNVLI ANNGIAAVKE IRSVRKWAYE TFGDEKAIQF TVMATPEDLA ANADYIRMAD
HYVEVPGGTN NHNYANVELI VDIAERMSVH AVWAGWGHAS ENPKLPESLA ASPKKIVFIG
PPGSAMRSLG DKISSTIVAQ HAKVPCIPWS GTGVDQVVID DSGLVTVADD IYLKGCVNSW
EEGLEKAKDI GFPVMIKASE GGGGKGIRQA MSEDGFEQLY KAAASEIPGS PIFIMKLAGN
ARHLEVQLLA DQYGNNVSLF GRDCSVQRRH QKIIEEAPVT IAKPPTFKSM EDAAVRLGRL
VGYVSAGTVE YLYSHEDDKF YFLELNPRLQ VEHPTTEMVS GVNLPVAQLQ VAMGIPLHRI
SDIRLLYGLD PKLTTEIDFN FEDTQSEKTQ RRPSPKGHCT ACRITSEDPG EGFKPSNGVM
HELNFRSSAN VWGYFSVSTA SSIHSFSDSQ FGHIFAYGEN RAASRKNMVV ALKELSIRGD
FRTTVEYLIK LLETEAFEDN TITTGWLDEL ISKKLTAERP DPMLAVICGA TTKAHIASEA
CIADYRSGLE RGQVPSKDIL KTVFTIDFIY EGVRYRFTAT RASVDSYHLF INGSKCSVGV
RALSDGGLLI LLDGRSHSVY WKEEVGATRV SVDSKTCLLE QENDPTQLRS PSPGKLVKYT
VENGEHVSAG QTYAEVEVMK MFMPLVAQED GMVQLIKQPG VTIEAGDILG ILALDDPSRV
KQAQSFLGQL PELGAPQVIG SKPSQKFDLL NSILKNILAG FDNSVIMQKS LKDFVDVLRD
PELPYSEWAA RHSAFHSRMP QKLDSAFTQI IDKAKSRHVE FPAKTLARTF AKFLDDNVSP
SDADTLKDTL APLTEVFESY AEGQKVHELR IIAGLLKEYA NVEALFSGSR NQSEEVILKL
RDENKENYLK VIQLVLSHSR VLNKNNLILA VLEEYRPNKP NVGNVGKHLR EALHKLTELE
SRGTAKVSLK AREILIQCAM PSLDERMGQM EHILRSSVVE NKYGETGWEH REPSLDIIKE
VVDSKYTVFD VLTSFFCHDD AWVSMAALEV YVRRAYRAYN LKTVHYHTDE NEGVPTFMSW
DFSLRKVGQF EFDIPIETNP SVPTTPKEFS FNRIHSISDM SYLTSRTNEE PIRKGVMIPC
RYMDEIEELL LKAFEVLPKH RKRPIPALAG RRNTGSGKSD DFELANVLNV AIVDTEDESD
QAMLARVKSI VHSFKDDLLS RRVRRVTFIC GHKDATYPAY YTFRGPEYEE DATLRHMEPA
LAFQLELGRL SLFKIHPVFT ENKSIYVYEG IGKAVETDKR YFTRAVIKPG RLRDDIPTID
YLISEADRVI NDIFDALEII GNNNSDLNHM FLNFTPVFQL KPEDVEHSLQ GFVDRFGIRA
WRLRVSQVEI RIICTDPVTG LPYPLRVIII NTSGYVIQIE IYAEKKSERG EMVFHSIGGT
TKIGSQHLLP VSTPYPTKNW LQPKRYKAHL LGTQYVYDFP ELFRQAIQNS WVKAVKAHPS
LAEKQPPTGE CIDYNELVLD DDDKLTEVAR EPGTNAHGMV GWLLKAYTPE YPKGRKFIIV
ANDITYKIGS FGPKEDHFFN KCTEMAQALG IPRIYLSANS GARLGLAEEL IPHFKVAWND
PEDQLRGFKY LYLDEEGKKR LGNDVITEEV TEDGEKHHKI TAVVGAEDGL GVECLRGSGL
IAGATSKAYN DIFTVTLITC RSIGIGAYLV RLGQRAVQVE GQPIILTGAG ALNNLLGREV
YTSNLQLGGT QIMYRNGVSH LTTNDDFAGV SKIVEWLSFV PAQRGLPVPI APSIDTWDRD
NIYTPPGKQP YDVRWLIGGK EDEDGFQPGL FDKNSFVETL GGWARTVVVG RARLGGIPMG
VIAVETRTVE NITPADPANP DSVEQVSNEA GGVWYPNSAF KTAQAINDFN YGEQLPLMIL
ANWRGFSGGQ RDMYNEVLKY GSYIVDALVK FEQPIFVYIP PFGELRGGSW VVVDPTINPV
AMEMYADVDS RAGVLEPEGI IGIKYKKEKQ LQTMARLDPT YASLKKEAAD PTLSKEQLED
VKAKLVARER QLLPIYAQIS LQFADLHDRA GRMKAKGTIR EVIEWKNARR FFYWRVRRRL
NEEYTLKRIS AAAGSSTSDI ESRRNNLRSL AAWTGVPDFD RNDKDVVTWY EENAATVAEK
VEHIKAQAVS TNMAGLLSSD KTSALKGLKD LLHNLPISER EDILKYLQ
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