ID A0A367Y9B4_9ASCO Unreviewed; 2223 AA.
AC A0A367Y9B4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:RCK62476.1};
GN Name=ACC1_1 {ECO:0000313|EMBL:RCK62476.1};
GN ORFNames=Cantr_08842 {ECO:0000313|EMBL:RCK62476.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK62476.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK62476.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK62476.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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:RCK62476.1}.
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DR EMBL; QLNQ01000025; RCK62476.1; -; Genomic_DNA.
DR STRING; 5486.A0A367Y9B4; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000253472; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000253472}.
FT DOMAIN 51..560
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 209..401
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 687..761
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1478..1812
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1816..2132
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT COILED 2162..2189
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2223 AA; 248237 MW; B68F41A3C5B233EE CRC64;
MTDLSPSPTD SLNYTQLHSS LPSHFLGGNS VLTAEPSAVT DFVKTHQGHT VITKVLIANN
GIGAVKEIRS VRKWAYETFG DERAIQFVAM ATPEDMEANA EYIRMADQFV EVPGGTNNNN
YANVDLIVEI AERTDVHAVW AGWGHASENP LLPERLAASP KKIVFIGPPG SAMRSLGDKI
SSTIVAQHAK VPCIPWSGTG VEEVHVDPET KLVSVDDHVY AKGCCTSPED GLEKAKRIGF
PVMVKASEGG GGKGIRKVDH EKDFISLYNQ AANEIPGSPI FIMKLAGDAR HLEVQLFADQ
YGTNISLFGR DCSVQRRHQK IIEEAPVTIA NKDTFVEMEK AAVRLGKLVG YVSAGTVEYL
YSYAEDKFYF LELNPRLQVE HPTTEMVSGV NLPAAQLQIA MGLPMHRIRD IRLLYGVDPH
SATEIDFEFK SPNSLITQRK PAPKGHCTAC RITSEDPGEG FKPSGGTLHE LNFRSSSNVW
GYFSVANQSS IHSFADSQFG HIFAFGENRQ ASRKHMIVAL KELSIRGDFR TTVEYLIKLL
ETPDFADNTI TTGWLDELIT KKLTAERPDP IVAVVCGAVT KAHIQAEEDK KEYIESLEKG
QVPNKSLLKT IFPVEFIYEG ERYKFTATKS SEDKYTLFLN GSRCVIGARS LSDGGLLCAL
DGKSHSVYWK EEAAATRLSV DGKTCLLEVE NDPTQLRTPS PGKLVKYLVE SGEHVDAGQS
YAEVEVMKMC MPLIAQENGT VQLLKQPGST LNAGDILAIL ALDDPSKVKH AKPYEGTLPE
MGDPTVTGSK PAHLFQHYDT ILKNILAGYD NQVILNSTLK NMMEILKNKE LPYSEWRLQI
SALHSRIPPK LDEALTSLIE RTESRGAEFP ARQILKLVNK TLGEPGNELL GDVVAPLVSI
ANRYQNGLVE HEYDYFASLV NEYCNVEHFF SGENVREEDV ILRLRDENKS DLKKVISICL
SHSRVSAKNN LILAILEAYE PLLQSNSSTA VAIRDSLKKI VQLDSRACAK VGLKARELLI
QCSLPSIKER SDQLEHILRS AVVETSYGEV FAKHREPKLE IIQEVVESKH VVFDVLSQFL
VHQDCWVAIA AAEVYVRRSY RAYDLGKIDY HIHDRLPIVE WKFKLAQIAG SRYNAVQSAS
VGDDSTTMKH AASVSDLSFV VDSKSESTSR TGVLVPARHL DDVDEILSAA LEYFQPSDAL
SFQAKGERPE LLNVLNIVIT DIDGYSDEDE CLKRIHEILN EYEDDLVFAG VRRVTFVFAH
QVGSYPKYYT FTGPVYEENK VIRHIEPALA FQLELGRLAN FDIKPIFTNN RNIHVYEAIG
KNAPSDKRFF TRGIIRGGVL KDEISLTEYL IAESNRLISD ILDTLEVIDT SNSDLNHIFI
NFSNVFNVQP ADVEAAFASF LERFGRRLWR LRVTGAEIRI VCTDPQGNSF PLRAIINNVS
GYVVKSELYL EVKNPKGDWV FKSIGHPGSM HLQPISTPYP VKESLQPKRY RAHNMGTTFV
YDFPELFRQA TISQWKKHGK KAPKDVFTSL ELITDENDAL VAVERDPGAN KIGMVGFKVT
AKTPEYPRGR SFIIVANDIT HKIGSFGPDE DEYFNKCTDL ARKLGVPRIY LSANSGARIG
VAEELIPLYQ VAWNEEGNPD KGFRYLYLNP DAKEALEKDG KGDTIVTERI VEDGQERHVI
KAIIGAENGL GVECLKGSGL IAGATSRAYR DIFTITLVTC RSVGIGAYLV RLGQRAIQIE
GQPIILTGAP AINKLLGREV YSSNLQLGGT QIMYNNGVSH LTASDDLAGV EKIMEWLSYV
PAKRGMPVPI LESEDTWDRD IDYYPPKQEA FDVRWMIEGK QVEGEEFESG LFDKGSFQET
LSGWAKGVVV GRARLGGIPI GVIGVETRTI ENMIPADPAN PSSTEALIQE AGQVWYPNSA
FKTAQAINDF NNGEQLPLMI LANWRGFSGG QRDMYNEVLK YGSFIVDALV DFKQPIFTYI
PPNGELRGGS WVVVDPTINS DMMEMYADVD SRAGVLEPEG MVGIKYRRDK LLATMQRLDP
TYAQLKEKLN DSSLSPEEHA QVSTKIVKRE KALLPIYAQI SVQFADLHDR SGRMMAKGVI
RKEIKWVDAR RFFFWRLRRR LNEEYVLKLI GEQVKNANKL EKVARLKSWM PTVDYDDDQA
VSTWIEENHA KLQKRVEELR QEKNKSDIVK LLQEDPSNAA SVMRDFVDRL SDEEKEKFLK
SLN
//
