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Database: UniProt
Entry: E5ACZ0_LEPMJ
LinkDB: E5ACZ0_LEPMJ
Original site: E5ACZ0_LEPMJ 
ID   E5ACZ0_LEPMJ            Unreviewed;      2279 AA.
AC   E5ACZ0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Similar to acetyl-CoA carboxylase {ECO:0000313|EMBL:CBY02342.1};
GN   ORFNames=LEMA_P011290.1 {ECO:0000313|EMBL:CBY02342.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY02342.1, ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(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}.
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DR   EMBL; FP929139; CBY02342.1; -; Genomic_DNA.
DR   RefSeq; XP_003845821.1; XM_003845773.1.
DR   STRING; 985895.E5ACZ0; -.
DR   EnsemblFungi; CBY02342; CBY02342; LEMA_P011290.1.
DR   GeneID; 13289567; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_1_1; -.
DR   InParanoid; E5ACZ0; -.
DR   OMA; DFEDNTI; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000002668; Genome.
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:UP000002668}.
FT   DOMAIN          56..564
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          208..405
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          691..765
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1515..1857
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1861..2176
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          429..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2279 AA;  253464 MW;  2D7E06FEBAE5461E CRC64;
     MADAAQNEAN GSASINGGLS ARAAQLAPHF IGGNHLNVAA PGKVKDFVAA NDGHTVITNV
     LIANNGIAAV KEIRSVRKWA YETFGDERAI QFTVMATPED LQANAEYIRM ADQYVEVPGG
     TNNNNYANVE LIVDVAERMN VHAVWAGWGH ASENPKLPES LAASPKKIVF IGPPGSAMRS
     LGDKISSTIV AQHAQVPCIP WSGSGVDEVL VDDQGIVTVE DHVYEKGCTK SWEEGLEKAK
     AIGFPVMVKA SEGGGGKGIR KVESEDNFEQ LYKAAASEIP GSPIFIMKLA GSARHLEVQL
     LADQYGNNIS LFGRDCSVQR RHQKIIEEAP VTVAGSKTFQ EMEKAAVSLG RLVGYVSAGT
     VEYLYSHSDD KFYFLELNPR LQVEHPTTEM VTGVNLPAAQ LQIAMGLPLH RIRDIRLLYG
     ADPHTSSPID FDFSNEGSGQ TQRRPTPKGH CTACRITSED PDEGFKPSGG TIHDLNFRSS
     SNVWGYFSVS SSGGIHSFSD SQFGHIFAYG ENRQASRKHM VVALKELSIR GDFRTTVEYL
     IKLLETPAFE DNTITTGWLD ELISKKLTAE RPDPMIAVIC GAVTKAHVAS EACFSEYKTS
     LEKGQVPSKD VLKTVFPIDF IYEGFRYKFT ATRSTIDSFT LFINGSKCSV GVRALADGGL
     LILLNGKSHN VYWKEEVGAT RLSVDGKTCL LEQENDPTQL RTPSPGKLVK FLVENGSHVG
     KGQPFAEVEV MKMYMPLIAS EAGMVNLIKQ PGAVLEAGDI LGVLALDDPS KVKSAQNFLG
     LLPDLGSPQV MGAKPPQRFV YLVHILRNIL QGYDNQVIMQ STLKELVDVL RDPELPYGEW
     NAQASALHAR MPQKLDTMLS QIVDKAHSRG LEFPSKALNK TFQKFLDENV PKGDAALLTS
     ALAPLNDVIV RYAEGLKAHE YSVMTSFLEQ YWSVESLFSS RASRDEEVIL KLRDANRDDI
     ASVVHTVLSH ARVSAKNNLI IAILDLYRPN RPGVGNIAKY FKSSLKKLTE LESKQTAKVS
     LKAREVLIQC AMPSLEERTA QMEHILRSAV VESKYGESGW EHREPNFEVI KEVVDSRYTV
     FDVLTQFFVH PDPWVSLAAL EVYTRRAYRA YQLQNINYHN EGEQSCFLSW EFILRKVGEA
     EYGLAVEPSE PGTPSTPGFE RPPRIQSLSD MTAWQHRLDG EPSRKGVVVP VEYLDDADEL
     ISRALDLFKN VGTSKKGGAS LREGLTLKRT PTSGLIDIKS SDELTGVLNI AVRDIEGFDD
     KEILSRIQPI VEDYKEELLS RRIRRISFIC GHKDGTYPGY YTFRGPRYEE DDSIRHVEPA
     LAFQLELGRL SKFNIKPVFT ENRNIHIYEA IGKGAESDKR YFLRAVVRSG RLREEIPTAE
     YMVSETDRLM TDILDALEIV GTSQADMNHI FINFSHVFPL NPSEVEEAIG GFLERFGRRL
     WRLRVTGAEI RIIVTDPATG IPYPLRVIIT NTSGYVIQVE MYAERKTENN NRWLFHSIGG
     TTKIGALHLQ PVSTPYPTKG ALQPKRYKAH LMGTQYVYDF PELFRQAVEN SWDVAVANVS
     SLRDKRPPKG ECTEYYELVL DDTENLVELN REPGNNSIGM VGWMVTAKTP EYPLGRRFII
     IANDITYKIG SFGPQEDKFF HKCSELARKN GIPRIYLSAN SGARIGLAEE LIPHFSVAWK
     NVDKPEAGFD YLYLTPEKYN HFVDGKRNDV ICEKIEVDGE TRYQITTVIG QEDGLGVESL
     RGSGLIAGET SRAYEDIFTI TLVTCRSVGI GAYLVRLGQR AIQIEGQPII LTGAQAINKL
     LGREVYTSNL QLGGTQIMYR NGVSHMTADD DFQGVSKIVK WLSYVPDMKG APVPTSPSSD
     DWDRDVAVYP PGKAAFDVRQ LITGKTDEDG FQPGLFDTGS FEESLGGWAK TVVVGRARLG
     GIPIGVIAVE TRSVENVTPA DPANPDSIEQ VTSEAGGVWY PNSAFKTAQA INDFNHGEQL
     PLMILANWRG FSGGQRDMYN EVLKYGSYIV DALVKFEQPV FVYIPPYGEL RGGSWVVVDP
     TINPEYMEMY ADEDSRGGVL EPEGLVGIKY RKERQLETMA RNDPTYGALK RKLNDPSTPQ
     DQLQSIKAEM TQREKLLLPV YGQIALQFAD LHDRAGRMQA KGVIRQALRW QNARRFFYWR
     LRRRLNEEYI LKKFAGAAQP SHTIAQPTPA TRTRGLDMLK HLCNMPNWET DDMGATMWYE
     GNRQVVADKL EQLKKEGIAM EIAQLMNQDR EGGLKGVMAM LSTLPTSEKE EVLKLLNKA
//
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