ID A2QZ87_ASPNC Unreviewed; 2283 AA.
AC A2QZ87;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Contig An12c0110, genomic contig {ECO:0000313|EMBL:CAK46172.1};
GN ORFNames=An12g04020 {ECO:0000313|EMBL:CAK46172.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK46172.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK46172.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270267; CAK46172.1; -; Genomic_DNA.
DR RefSeq; XP_001395476.1; XM_001395439.2.
DR EnsemblFungi; CAK46172; CAK46172; An12g04020.
DR GeneID; 4985750; -.
DR KEGG; ang:An12g04020; -.
DR VEuPathDB; FungiDB:An12g04020; -.
DR HOGENOM; CLU_000395_5_2_1; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000006706; Chromosome 3L.
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:UP000006706}.
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; 254540 MW; E5F7964C2F6D37E7 CRC64;
MSAPNGHPSA RAAQHNLASH FIGGNNLNAA PPSSVKDFVA SHEGHSVISS VLIANNGIAA
VKEIRSVRKW AYETFGNERA IQFTVMATPE DLHANADYIR MADQYVEVPG GTNNNNYANV
DLIVDVAERM DVHAVWAGWG HASENPRLPE ALAASPKRII FIGPPASAMR SLGDKISSTI
VAQHAGVPCI PWSGTGVDDV RIDDKGIVTV DDDVYNRGCT FSPEEGLEKA 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 GQLPELGPPQ
VVGSKPPQRF FLLHSILENI LKGYDNQVIM NATLKELVEV LRNPDLPYGE WNAQSSALHS
RMPQKLDSQL QNIVDKARAR 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 ASGEVPILSW DFTLDKLGQP EFGPVTTDPS
TPSTPTAEMN PFKRINSISD MSYLVGDGSE PMRKGAIIPV QYLEDAEEFL PRALEIFPRA
GSKKKASDNG LLANLEGKRR PAPRVENENE LTGVLNVAIR DVEDLDDNQI VSQINNMLAD
LKEELLARRI RRVTFICGKN GIYPGYFTFR GPNYDEDESI RHNEPALAFQ LELGRLSKFK
IKPVFTENRN IHVYEAIGKG PENDKAVDKR YFVRAVVRPG RLRDDIPTAE YLTSEADRLM
NDILDALEII GNNNSDLNHI FINFSPVFNL QPKDVEEALA GFLERFGRRL WRLRVTGAEI
RILCTDPVTG VPYPLRVIIT NTYGFIIQVE LYIEKKTEKG EWIFHSIDGG SNKLGSMHLR
PVSTPYPTKE WLQPKRYKAH LMGTQYVYDF PELFRQAFQN SWTKAIANIP SLADQRPPVG
ECIDYSELVL DDTDNLVEIS RGPGTNTHGM VGWIVTARTP EYPRGRRFII VANDITFQIG
SFGPAEDKFF HKCTELARKL GIPRIYLSAN SGARIGMADE LIPYFSVAWN DPENPAAGFK
YLYFTPEVKQ KLDASKKKEV ITEEIQDEGE VRHKITTVIG AKDGLGVECL KGSGLIAGAT
SKAYEDIFTI TLVTCRSVGI GAYLVRLGQR AIQVEGQPII LTGAPAINKL LGREVYTSNL
QLGGTQIMYR NGVSHMTAND DFEGVQKIVE WMSFVPDRKG APIPIRPWSD TWDRDVAYYP
PAKQPYDPRW LIAGKEDEEG FLPGLFDTGS FEEALGGWAR TVVVGRARLG GIPMGVIAVE
TRSVENVTPA DPANPDSMEM VANEAGGVWY PNSAYKTAQA LRDFNNGEQL PVMILANWRG
FSGGQRDMYN EVLKYGSYIV DALVKYEQPI FIYIPPHGEL RGGSWVVVDP TINPDQMEMY
ADVEARGGVL EPEGIVNIKY RRDKQLDTMA RLDATYGELR RSLEDPSLSK EQLSDVKAKM
AAREEQLLPV YLQIALQFAD LHDRAGRMEA KNTIRHPLTW KNARRFFYWR LRRRLSEELI
VKRMVAAAPN PAARDGSVAI PAGSNAPVST ESARAVHLRT LHGWTGLLDD ELQREDQRVA
TWYEENKKAI QTKVDSLKAE SVATEVAQLL VNNRDGALKG VQQILSVLPV EEKEAVLKYL
SSN
//
