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Database: UniProt
Entry: A0A010R0B5_9PEZI
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ID   A0A010R0B5_9PEZI        Unreviewed;      2282 AA.
AC   A0A010R0B5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:EXF85967.1};
GN   ORFNames=CFIO01_05902 {ECO:0000313|EMBL:EXF85967.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF85967.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF85967.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF85967.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXF85967.1}.
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DR   EMBL; JARH01000045; EXF85967.1; -; Genomic_DNA.
DR   RefSeq; XP_007590342.1; XM_007590280.1.
DR   STRING; 1445577.A0A010R0B5; -.
DR   KEGG; cfj:CFIO01_05902; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_0_1; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000020467; 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:UP000020467}.
FT   DOMAIN          59..567
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          216..408
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          694..768
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1521..1859
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1863..2178
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          437..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2282 AA;  254122 MW;  8615E101DB8829B0 CRC64;
     MTEITAANGT GRTVPHVNGK ATYAEKHKIA DHFIGGNKLS NAPASKVKDF VAQQDGHTVI
     TNVLIANNGI AAVKEIRSVR KWAYETFGDE KAIQFTVMAT PEDLAANADY IRMADHYVEV
     PGGTNNHNYA NVELIVDIAE RMNVHAVWAG WGHASENPKL PESLAASPKK IVFIGPPGSA
     MRSLGDKISS TIVAQHAKVP CIPWSGTGVD AVEVDNQGIV TVADDIYSKG CVTSWQEGLE
     KAKAIGFPVM IKASEGGGGK GIRKALSEDG FEQLYKAAAG EIPGSPIFIM KLAGNARHLE
     VQLLADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAKDI TFKAMEDAAV RLGRLVGYVS
     AGTVEYLYSH ADDKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGI PLHRIRDIRL
     LYGVDPRTST EIDFEFKQEG SEKTQRRPRP KGHTTACRIT SEDPGEGFKP SNGVMHDLNF
     RSSSNVWGYF SVSTASSIHS FSDSQFGHIF AYGENRAASR KHMVVALKEL SIRGDFRTTV
     EYLIKLLETE AFEDNTITTG WLDELITKKL TAERPDPMLA VVCGAVTKAH LFSEECMTEY
     RTSLEKGQVP SKDILKTVFA IDFIYEGFRY KFTATRASVD SYHLFINGSK CSVGVRVLSD
     GGLLILLDGR SHSVYWKEEV GATRLSVDGK TCLLEQENDP TQLRTPSPGK LVKYLVENGE
     HVKAGQPFAE VEVMKMYMPL IASEDGLVQL IKQPGATLEA GDILGILALD DPSRVKQASP
     FVGQLPVYGE PVAVGTKPAQ RFDLLHNTLK NILLGYDNSV IMAATLKQLI EVLRTPELPF
     SQWNAQFAAL HSRMPQKLDA QFTQIVDRAK SRHADFPAKA LAKAFQKFLE DNVAAGDAEM
     LKTTLAPLTD VLNAYSEGTK AHELTVIKDL LGSYIEIERL FTGYGTQEDS VILKLRDQNK
     DDIRKVVQTV LSHSRVGAKS SLILAILEEY RPNKPNVGNV AKYLRTALQQ LTELQSSRTT
     SKVSLKAREI MIQCSLPSLE ERTAQMEHIL RSSVVESRYG EAAWDHREPS LEVIKEVVDS
     KYTVFDVLTL FFAHEDPWVS LAALEVYVRR AYRAYILKQI EYHSDETDTP LFCTWDFALR
     KIGQSEYGLP LQSAAPSSPA TPSGSGGSFD FKRIHSISDM SYLNHKWDSE PNRKGVIVPV
     KYLDDAEDLL GKALETLTVS EKARKRSTPG LIPDLSGKRK PAAPKVDSDE LSAVINVAVR
     DAESKSDQEI LSRIVPIVEQ FKEELLNRNV RRITFICGRN DGAYPGYYTF RGPEYVEDDS
     IRHSEPALAF QLELGRLAKF HIKPVFTENK NIHVYEGVGK AVDGDKRYFT RAVIRPGRLR
     DEIPTAEYLI SEADRVINDI FDALEIIGNN NSDLNQVFIN FTPVFQLHPQ EVESSLQGFL
     DRFGARAWRL RVAQVEIRII CTDPDTGVPY PLRVIITNTS GYVVDVDIYA ERKSEKGEWV
     FNSIGGTKEK GPMHLLPVST PYATKNPLQP KRYKAHLMGT QYVYDFPELF RQAIQNSWTQ
     SVKKHGALGA QQPKSGECVS YTELVLDDKD TLQEVNREPG TNTCGMVGWI FNAKTPEYPK
     GRKFIVVAND ITYMIGSFGP KEDNFFYKCT ELARKLGIPR IYLSANSGAR LGVANELMPY
     FKVAWNDANK QDNGFKYLYL DDEAQKRFAK DVITEEISED GEKRHKIVTI VGQEDGLGVE
     CLRGSGLIAG ATSKAYNDIF TITLVTCRSV GIGAYLVRLG QRAVQIEGQP IILTGAPALN
     NVLGREIYTS NLQLGGTQIM YRNGVSHMTG TDDFDGVSKI VEWMSFIPEK RGSPIPVSPS
     TDGWDRDVVY TPPQKQAYDV RWMIGGHPTD NGGFEAGLFD KDSFVETLGG WARTVVVGRA
     RLGGIPMGVI AVEARSVENI TPADPANPDS IEQITNEAGG VWYPNSAFKT AQAINDFNNG
     EQLPLMILAN WRGFSGGQRD MYNEVLKYGS YIVDALVKYE QPIFVYIPPF GELRGGSWVV
     VDPTINPEAM EMYADVDARG GVLEPEGIIG IKYRKDKQLE TMARLDPVYA SLKKQMTADL
     PKEQADEIKK KMTIREKQLL PVYSQVAIQF ADLHDRAGRM KAKGVIRDQL EWVNSRRYFY
     WRLRRRLNEE YLLKRMSSTV LTSTPGNDKS KAPETRSRNL QLLESWSGVV NFSTADREVA
     EWYEANRKSV TDRIETVKAD NLAADLSSVL RANKSAAMRG VRDVIRTMPP EERDQLLKYL
     RD
//
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