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Database: UniProt
Entry: A0A2V1CA34_9HELO
LinkDB: A0A2V1CA34_9HELO
Original site: A0A2V1CA34_9HELO 
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
//
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