ID R7YUQ2_CONA1 Unreviewed; 2282 AA.
AC R7YUQ2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:EON65635.1};
GN ORFNames=W97_04874 {ECO:0000313|EMBL:EON65635.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON65635.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; JH767575; EON65635.1; -; Genomic_DNA.
DR RefSeq; XP_007780952.1; XM_007782762.1.
DR STRING; 1168221.R7YUQ2; -.
DR GeneID; 19902185; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000016924; 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}; Reference proteome {ECO:0000313|Proteomes:UP000016924}.
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 1519..1861
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1865..2180
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 439..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2282 AA; 254082 MW; B60F1BC4008E4F3C CRC64;
MADTNGVNGV NGHDGYPSAN AAKYNLAPHF IGGNHLGVAS PGKVKEFVAA NGGHTVITNV
LIANNGIAAV KEIRSVRKWA YETFGDERAI QFTVMATPED LQANADYIRM ADQYVEVPGG
TNNNNYANVE LIVDVAERMG VQAVWAGWGH ASENPKLPES LAASPHKIVF IGPPGSAMRS
LGDKISSTIV AQHAKVPCIP WSGEGVDQVL VGDDGIVTVE DHVYDKGCTH SPEEGLEMAR
KIGFPVMIKA SEGGGGKGIR KADTEEGFHN LYRAAASEIP GSPIFIMKLA GNARHLEVQL
LADQYGNNIS LFGRDCSVQR RHQKIIEEAP VTVANPNTFH AMEKAAVSLG KLVGYVSAGT
VEYLYSHADD KFYFLELNPR LQVEHPTTEM VSGVNLPAAQ LQIAMGLPLS RIRDIRLLYG
ADPHSATEID FDFTKEGSLQ NQRKPTPKGH TTACRITSED PGEGFKPSSG TMHELNFRSS
SNVWGYFSVG TAGGIHNFSD SQFGHIFAYG ENRAASRKHM VVALKELSIR GDFRTTVEYL
IKLLETPAFE DNTITTGWLD ELISKKLTAE RPDPMVAVIC GAVTKAHIAS DIAMTEYRTS
LEKGQVPSKD VLKTVFPVDF IYEGHRYKFT ATRSSIDSYT LFINGSKCAV GVRALADGGL
LVLLGGKSHN IYWREEVGAT RLSVDSKTCV LEQENDPTQL RTPSPGKLVK FTIENGEHVR
KGQAFAEVEV MKMYMPLIAQ EDGIVNLIKQ PGATLEAGDI LGILALDDPS KVKSAQPFLG
QLPDLGAPQV MGNKPPQRFT YLYNILRDIL QGFDNQVIMQ STLKELVEVL RNPELPYGEW
NAQASALHAR MPQKLDSTLG QIVERAHSRN LEFPAKQLAK AFTRFLEENV EPSDANLLRS
ALVPLIEVID RYKDGLKVHE YDVMVSLLEQ YYEVESLFSS RTNRDEEVIL KLRDENKDNI
AKIVVTVLSH TRASSKNHLI IAILDTYRPN RPGVGNVAKY FKFALKKLAE LESRATAKVA
LKAREVLIQC AMPSLEERTS QMEHILRSSV VESRYGESGW DHREPNFDVI KEVVDSRYTV
FDVLPQFFAH SDPWVALAAL EVYTRRAYRA YLLKKIEYHV ENEAPYILSW DFALRKVGES
EFGLPIESSH PSTPSTPAGE SPFKRIHSIS DLSYIGKAAE GETTRKGAVV PVPFIDDAEE
YLTRALEVFP SVGSYRKRNS SANNAGLMAE LSRNRRPAPP KLENEDELTA VCNVAVRDAE
SFDDKEILDR ILPIVNEYKE EMLARRVRRL TFICGHKDGT YPGYYTFRGP AYEEDASIRH
IEPALAFQLE LGRLSKFNIK PVFTENRNIH IYEAVGKGAE NDKRYFTRAV VRPGRLREDI
PTAEYMISEA DRLMTDILDA MEIIGNNNSD MNHIFINFST VFPLAPREVE EALGGFLDRF
GRRAWRLRVT GAEIRIVCTD PQTGAPYPLR VVITNTSGYI IQVELYAERK SDKGGQWLFH
SIGGTTKIGS MHLRPVNTPY PTKGALQPKR YKAHIMGTQY VYDFPELFRQ AVENSWHQVV
AKHGHLKDKQ PVQGECIEYN ELVLDEDDNL AEVNRDPGSN TIGMVGWIVT AKTPEYPRGR
RFIIIANDIT FKIGSFGPAE DKFFHKCSEL ARKLGIPRIY LSANSGARIG MAEELIPHFS
VAWNDPSNPA KGFKYLYLTP EKNKRFTEGN KRDVITEKIV EDGETRYKIT TIIGAEDGLG
VECLKGSGLI AGETSRAYED IFTITLVTCR SVGIGAYLVR LGQRAIQIEG QPIILTGAPA
INKLLGREVY TSNLQLGGTQ IMYNNGVSHM TAEDDFSGVS KIVKWLGFVP DKKGNPVPIS
PTIDNWDRDV TYYPPQKQPY DVKWLIAGKE DDEGFLSGLF DRGSFEETLG GWAKTVVVGR
ARLGGIPMGV IGVETRSVTN VTPADPANPD SIEQVTSEAG GVWYPNSAFK TAQAINDFNH
GEQLPLMILA NWRGFSGGQR DMYNEVLKYG SMIVDALVKY EQPIFVYIPP FGELRGGSWV
VVDPTINPQV MEMYADEDAR GGVLEPEGIV GIKFRKDRQL ETMARLDATY GDLKRRLADP
ATPRSELADI KARMTEREHA LLPVYAQISL QFADLHDRAG RMEAKGVIRK PLRWREARRF
FYWRLRRRLN EEYILKRMAA VASKDVGSLS PTAARATHLE LLKSWSDVPN FEKDDMSVAV
WYEENRKQVS EKVEGMKRAG IAEDVAGLVR RDKEGALEGF KTALSMLPTG EKEELLRMLS
RV
//
