ID G7XHM5_ASPKW Unreviewed; 2283 AA.
AC G7XHM5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:GAA86434.1};
GN ORFNames=AKAW_04548 {ECO:0000313|EMBL:GAA86434.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA86434.1};
RN [1] {ECO:0000313|EMBL:GAA86434.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA86434.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF126456; GAA86434.1; -; Genomic_DNA.
DR STRING; 1033177.G7XHM5; -.
DR VEuPathDB; FungiDB:AKAW_04548; -.
DR eggNOG; KOG0368; Eukaryota.
DR InParanoid; G7XHM5; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000006812; 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}.
FT DOMAIN 47..555
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 199..396
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 682..756
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1505..1847
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1851..2166
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 428..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2283 AA; 254772 MW; C6EABF7FBD17A4C7 CRC64;
MSAPNDHPSA RAAQHNLASH FIGGNNLNAA PPSSVKDFVA SHEGHSVISS VLIANNGIAA
VKEIRSVRKW AYETFGNERA IQFTVMATPE DLHANADYIR MADQYVEVPG GTNNNNYANV
DLIVDVAERM DVHAVWAGWG HASENPRLPE ALAASPKRII FIGPPASAMR SLGDKISSTI
VAQHAGVPCI PWSGTGVDDV RIDDKGIVTV DDDVYNRGCT FSPEEGLQKA KEIGFPVMIK
ASEGGGGKGI RKVEREEDFI SLYNAAANEI PGSPIFIMKL AGNARHLEVQ LLADQYGNNI
SLFGRDCSVQ RRHQKIIEEA PVTIAKPITF QAMERAAVSL GRLVGYVSAG TVEYLYSHAD
DKFYFLELNP RLQVEHPTTE MVSGVNLPAA QLQIAMGIPL HRIRDIRLLY GVDPNTSGEI
DFDFSNEESF QTQRRPQPKG HTTACRITSE DPGEGFKPSS GTMHELNFRS SSNVWGYFSV
GTAGGIHSFS DSQFGHIFAY GENRSASRKH MVIALKELSI RGDFRTTVEY LIKLLETPAF
EDNTITTGWL DQLISNKLTA ERPDTIVAVL CGAVTKAHQA SEAGVEEYRK GLEKGQVPSK
DVLKTVFPVD FIYEGQRYKF TATRASLDSY HLFINGSRCS VGVRALADGG LLVLLNGRSH
NVYWKEEPAA TRLSVDGKTC LLEQENDPTQ LRTPSPGKLV KFTVENGEHV KAGQPFAEVE
VMKMYMPLIA QEDGIVQLIK QPGATLEAGD ILGILALDDP SRVKHAQPFT GQLPDLGPPQ
VVGSKPPQRF FLLHSILENI LKGYDNQVIM NATLKELVEV LRNPDLPYGE WNAQSSALHS
RMPQKLDSQL QTIVDKARAR KAEFPAKQLQ KTVQRFIEEN VNPADAEILK TTLLPLTEVI
NKYLDGLKVH EFNVFIGLLE QYYEVEKLFA GRNLRDEDSI LKLRDENKED IGKVVQTVLS
HSRIGAKNNL ILAILAMYRP NQPNVGNVSK YFKPILKKLT EFESRAAAKV TLKARELLIQ
CALPSLEERL SQMELILRSS VVESSYGETG WEHREPDSQV LKEVVDSKYT VFDVLPRFFV
HQDVWVTLAA LEVYVRRAYR AYTVKGIQYS ASGEVPLLSW DFTLDKLGQP EFGPITTDPS
TPSTPTAEMN PFKRINSISD MSYLVGDGNE PMRKGAIIPV QYLEDAEEFL PRALEIFPRA
GSKKKASDNG LLANLEGKRR PAPRVENENE LTGVLNVAIR DVEDLDDNQI VSQINNMLAD
LKEELLARRI RRVTFICGKN GIYPGYFTFR GPNYDEDESI RHNEPALAFQ LELGRLSKFK
IKPVFTENRN IHVYEALGKG PENDKAVDKR YFVRAVVRPG RLRDDIPTAE YLTSEADRLM
NDILDALEII GNNNSDLNHI FINFSPVFNL QPKDVEEALA GFLERFGRRL WRLRVTGAEI
RILCTDPVTG VPYPLRVIIT NTYGFIIQVE LYIEKKTEKG EWIFHSIDGG SNKLGSMHLR
PVSTPYPTKE WLQPKRYKAH LMGTQYVYDF PELFRQAFQN SWTKAIAKIP SLADQRPPVG
ECIDYSELVL DENDNLVEIS RGPGTNTHGM VGWIVTARTP EYPRGRRFII VANDITFQIG
SFGPAEDKFF HKCTELARKL GIPRIYLSAN SGARIGMADE LIPYFSVAWN DPENPAAGFK
YLYFTPEVKQ KLDASKKKEV ITEEIEDEGE VRHKITTVIG AKDGLGVECL KGSGLIAGAT
SKAYEDIFTI TLVTCRSVGI GAYLVRLGQR AIQVEGQPII LTGAPAINKL LGREVYTSNL
QLGGTQIMYR NGVSHMTAND DFEGVQKIVE WMSFVPDRKG APIPIRPWSD TWDRDVAYYP
PSKQPYDPRW LIAGKEDEEG FLPGLFDTGS FEEALGGWAR TVVVGRARLG GIPMGVIAVE
TRSVENVTPA DPANPDSMEM VANEAGGVWY PNSAYKTAQA LRDFNNGEQL PVMILANWRG
FSGGQRDMYN EVLKYGSYIV DALVKYEQPI FIYIPPHGEL RGGSWVVVDP TINPDQMEMY
ADVEARGGVL EPEGIVNIKY RRDKQLDTMA RLDATYGELR RSLEDQSLSK EQLSDIKAKM
AAREEQLLPV YLQIALQFAD LHDRAGRMEA KNTIRHPLTW KNARRFFYWR LRRRLSEELI
VKRMVAAAPN PAARDGSVAI PAGSNAPVST ESARAVHLRT LHSWTGLLDE ELQREDQRVA
TWYEENKKAI QTKVDSLKAE SVATEVAQLL LNNRDGALKG VQQILSVLPV EEKEAVLKYL
SSN
//
