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
//