ID A0A2V1CA34_9HELO Unreviewed; 2281 AA.
AC A0A2V1CA34;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative acetyl-CoA carboxylase {ECO:0000313|EMBL:PVH82526.1};
GN ORFNames=DL98DRAFT_653254 {ECO:0000313|EMBL:PVH82526.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH82526.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH82526.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH82526.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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; KZ804132; PVH82526.1; -; Genomic_DNA.
DR STRING; 1485229.A0A2V1CA34; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000244409; 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:UP000244409}.
FT DOMAIN 63..571
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 215..412
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 698..772
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1524..1866
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1870..2185
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 443..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2281 AA; 254075 MW; 90088F26F3F22DB1 CRC64;
MAAVNGKGNG VKATNGTVPI MNGSTSYAAK HKLADHFIGG NKLENAAPGP VKDFVAAHDG
HTVITNVLIA NNGIAAVKEI RSVRKWAYET FGDERAIQFT VMATPEDLQA NADYIRMADQ
YVEVPGGTNN NNYANVELIV DVAERMNVHA VWAGWGHASE NPKLPESLAA SPKKIVFIGP
PGSAMRSLGD KISSTIVAQH AKVPCIPWSG TGVDQVDVAE DGIVTVEDDV YMKGCVQSWQ
EGLEKAKQIG FPVMIKASEG GGGKGIRKAE SEQGFEALYK AAASEIPGSP IFIMKLAGNA
RHLEVQLLAD EYGNNISLFG RDCSVQRRHQ KIIEEAPVTI AKPETFQAME KAAVRLGRLV
GYVSAGTVEY LYSHSDDKFY FLELNPRLQV EHPTTEMVSG VNLPAAQLQI AMGLPLHRIR
DIRLLYGADP QTSSEIDFDF SKENSSLTQR RPKPKGHTTA CRITSEDPGE GFKPSSGTMH
ELNFRSSSNV WGYFSVGTAG GIHSFSDSQF GHIFAYGENR SASRKHMVVA LKELSIRGDF
RTTVEYLIKL LETPAFEGNT ITTGWLDELI SNKLTAERPD PMLAVVCGAV CKAHIASEAC
ITEYRNSLEK GQVPAKDILK TVFPIDFIYD GHRYKFTATR SSLDSYHLFI NGSKCSVGVR
ALSDGGLLVL LSGRSHNLYW KEEVGATRLS VDSKTCLLEQ ENDPTQLRTP SPGKLVKFTV
DNGEHIKAGQ AFAEVEVMKM YMPLIAGEDG IVQFIKQPGA TLEAGDIIGI LALDDPSRVQ
SAQPFLGHLP DLGPPQVVGT KPAQRFLLLH SVLANILNGF DNQVIMASTL KELIEVLRDP
DLPYGEWNAQ FSALHARMPQ RLDATFTQIV DRARVRKGEF PAKNLSKAFA KFLEENVAPS
DVETLKTTLL PLTEVLDRYA EGQKVHEFDV FSGLLEQYVS VEKLFSGRQS RDEEVVLKLR
DENKDDSFKV VQIVLSHSRI GAKNNLILAI LDEYKPNKPS AGNVAKYFRP ALRKLTELES
RQTAKVALKA RELLIQCAMP SLEERAAQME HILRSSVVES RYGETGWEHR EPDLEVLKEV
VDSKYTVFDV LPIFFGYQDP WVSLAALEVY IRRAYRAYSL KKIEYHNDSA EPPFIVSWDF
VLRKVGASEF GMPIQSSAPS TPATPSYESG NPFKRVSSIS DMSYLVNKTD NEPTRKGVIV
PVQYLDEAEE YLLRALEVFP SAGKTKKSAA SGLMPDLNGK RKTLPPIATE DELTAVCNVA
VRDSESLDDN ETIARINLIV KEYKEELLAR RIRRLTFICG HKDGSYPGYY TFRGPEYEED
QSIRHIEPAL AFQLELGRLS KFRIKPVFTE NRNIHIYEAT GKDVEGDKRY FTRAVVRPGR
LRDEIPTAEY LISESDRLMN DLLDALEIIG NNNSDLNHIF INFSPVFPLQ PPEVEKALGG
FLERFGRRLW RLRVTAAEIR IICTEPTTGM PYPLRVVITN TSGYVIQVEM YAERKSEKGG
DWVFQSIGGT TKVGSMHLRP VSTPYPTKEW LQPKRYKAHI MGTQYVYDFP ELFRQAIQTS
WVKAVSKHAS LADKQPPTGE CIDYSELVLD DKDNLAEVFR EPGTNTHGMV GWIVTARTPE
YPRGRKFVIV ANDITFKIGS FGPKEDQFFN KCTELARKLG IPRIYLSANS GARIGMAEEL
IPHFNIAWNN PDKPEAGFKY LYLKADAKKR FEDGKSKDVI TEEVNEDGEV RHKIVTIVGA
EDGLGVECLK GSGLIAGATS RAYEDIFTIT LVTCRSVGIG AYLVRLGQRA IQIEGQPIIL
TGAPAINKLL GREVYTSNLQ LGGTQIMYKN GVSHMTANDD FEGVSKIVEW MAYVPDKRNS
PLPIGPAVDS WDRDIVYTPP PKQPYDVRWL IAGKDDDEGF MPGLFDKDSF VETLGGWAKT
VVVGRARLGG IPMGVIAVET RSVENITPAD PANPDSMEQI TNEAGGVWYP NSAFKTAQAI
KDFNNGEQLP LMILANWRGF SGGQRDMYNE VLKYGSYIVD ALVKYEQPIF VYIPPFGELR
GGSWVVVDPT INPEFMEMYA DEDARGGVLE PEGIVNIKYR RDKQLETMAR LDPEYGSLRK
QLADKSLTPD QISAVKVKAT AREQLLLPVY MQVSLQFADL HDRAGRMKAK DVIRQSLVWR
ESRRFFYWRV RRRVNEEYIL KRMASASKNP LASRARNLET LAAWTGIPKF PHADREVAMW
YEENRKTVHE KVESLKTEGV AFDVASLLRG NSKGGLKGVQ QVLSMLPANE REDALRFLSQ
A
//