ID H8WWH3_CANO9 Unreviewed; 2218 AA.
AC H8WWH3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Acc1 acetyl-coenzyme-A carboxylase {ECO:0000313|EMBL:CCG20797.1};
GN ORFNames=CORT_0A04090 {ECO:0000313|EMBL:CCG20797.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG20797.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG20797.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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; HE681719; CCG20797.1; -; Genomic_DNA.
DR RefSeq; XP_003866237.1; XM_003866189.1.
DR GeneID; 14537690; -.
DR KEGG; cot:CORT_0A04090; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000005018; Chromosome 1.
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}.
FT DOMAIN 50..559
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 208..400
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 686..760
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1475..1809
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1813..2128
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2218 AA; 247676 MW; 7DD8E04C2548C847 CRC64;
MSESPTPSVM SDYSLLHNNL APHFLGLNSV SKAEPSKVTD FVKSHQGHTV ITRILIANNG
IAAVKEIRSV RKWAYETFGD ERAIQFTVMA TPEDLEANAE YIRMADQFVE VPGGTNNNNH
ANVDLIVDIA ENTDAHAVWA GWGHASENPL LPERLAASPK KIIFIGPPGS AMRSLGDKIS
STIVAQHADV PCIPWSGTGV DEVRVDPETN LVSVTDDVYA KGCCTSPEDG LEKAKQIGFP
VMIKASEGGG GKGIRKVESE ENFVTLYNQA ANEIPGSPIF IMKLAGDARH LEVQLLADQY
GTNISLFGRD CSVQRRHQKI IEEAPVTIAK KETFTEMEKA AVRLGKLVGY VSAGTVEYLY
SHAEDKFYFL ELNPRLQVEH PTTEMVTGVN LPAAQLQIAM GIPMHRIRDI RTLYGADPHS
ATEIDFEFST ENAVVSQRRP SPKGHCTACR ITSEDPGEGF KPSGGSLHEL NFRSSSNVWG
YFSVSNQSSI HSFSDSQFGH IFAFGENRQA SRKHMVVALK ELSIRGDFRT TVEYLIKLLE
TPDFEDNTIT TGWLDELITK KLTAERPDRI VAIVCGAVTK AHIQAEEEEK EYIQSLERGQ
VPHKNLLKTI FPVEFIYEGE RYKFTATKSS DDTYTLFLNG SRCTVGARPL SDGGLLCALG
GKSHAVYWKE EAAATRLSVD GKTCLLEVEN DPTQLRTPSP GKLVKYLVES GDHVNAGDTF
AEIEVMKMCM PLIAQENGVV QLIKQPGSTV NAGDMLAILA LDDPSKVKHA KPFEGTLPDM
GAPNVRGSKP AHKFNDYAAI LRNILAGYDN QVIMNTTLKK IVEVLKDREL PYSEWQQCIS
ALHSRLPIKL DESLTSLIER TKSRNADFPA RQILKQIGKA LSEEGALKDI VAPLVAIATR
YEKGLVEHEY DFFASLIDEY YNVESLFVGT NVREDDVLLK LRDENKSDLK KVISISLSHS
KVSAKNNLII AILQEYEPLL QSNSSVAASI RDSLKKLASL DSRGCAKVAL KAREILIQCS
LPSIKERSDQ LEHILRSSVL QTSYGEMYAK HREPNLDIIQ EVVDSKHIVF DVLSQFFVNT
DEWVAIAASE VYVRRSYRAY QLGKIEYDFH DQLPIIEWKF RLPSIANSRF NAIQQPATEE
ENTSMKHSAS VSDLSFVVDS KTDQMERTGV LVPCRHLDDA DEMLSAALEK LQPSDALTFQ
AGEEQTELLN VLNIVINNID GYADEKEYLE RVKDLLGEYK EDLVKASVRR ISFVFAHQVG
SYPKYYTFTG PDYLENKVIR HIEPALAFQL ELGRLANFDI KPIFTNNRNI HVYEAVGKNA
PADKRFFTRG IIRTGVIKDD ISISEYLIAE SNRLMSDILD TLEVVDTSNS DLNHIFINFS
NVFNIQPAEV EAAFGSFLER FGRRLWRLRI TGAEIRIVCA DSKGNALPLR AIINNVSGYV
VKSDLYLEMK NAKGDWVFKS IGHPGPMHLR PISTTYPVKE SLQPKRYKAH NMGTTYVYDF
PELFRQATLS QWKKYGQKAP NDVFTSLELI PDENGGLTAL ERDPGSNKIG MVGFLVTAKT
PEYPRGRQFV IVANDITHKI GSFGPEEDNF FNKCTELARE KGVPRIYLSA NSGARIGIAE
ELIPLFQVAW NKDGKPEEGF KYLYLTPEAK HAIDEDGKGN TLVTERAVEE GQERYIIKAI
VGAEDGLGVE CLRGSGLIAG ATSKAYKDIF TITLVTCRSV GIGAYLVRLG QRAIQVEGQP
IILTGAPAIN KMLGKEVYSS NLQLGGTQIM YRNGVSHLTA NDDLEGVEKI MEWLSYVPAK
RGLPVPILDS EDPWDRDVDY FPPKQESFDV RWMIEGKETD NGFESGLFDK DSFQETLSGW
AKGVVVGRAR LGGIPIGVIG VETRTVDNLI PADPANPNST ESLVHEAGQV WHPNSAFKTA
QAINDFNYGE QLPLMIMANW RGFSGGQRDM YNEILKYGSF IVDALVDFKQ PIFTYIPPFG
ELRGGSWVVV DPTINEEMME MYADVDSRGG VLEAEGLVSI KYRRDKLLAT MERLDTKYAE
LKSKINDPSL TPEEHSEVSR KLTVREKALL PIYAQISVQF VDLHDRSGRM LAKGVIRGEV
KWSDARRFFF WRLRRRLNEE YVLKMIGAQL KNSSKLEKVA RLKSWMPAVN YDDDQEVSNW
IEEHHSKLTK RLEELKHDAT RADLMKLLSN DSGAALAAVK EYLEKLPQES KSDFLNSL
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