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
//