ID A0A1L9PIV1_ASPVE Unreviewed; 2283 AA.
AC A0A1L9PIV1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJJ01421.1};
GN ORFNames=ASPVEDRAFT_41004 {ECO:0000313|EMBL:OJJ01421.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ01421.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878128; OJJ01421.1; -; Genomic_DNA.
DR STRING; 1036611.A0A1L9PIV1; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_41004; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000184073; 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:UP000184073}.
FT DOMAIN 48..556
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 200..397
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 683..757
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 427..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2171..2197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2182..2197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2283 AA; 254342 MW; DD33874C8EF048A7 CRC64;
MGDGATPSGV SRAAKYNLPS HFIGGNHLDA AAPSSVKDFV AQHEGHSVIT SVLIANNGIA
AVKEIRSVRK WAYETFGNER AIQFTVMATP EDLTANADYI RMADQYVEVP GGTNNNNYAN
VELIVDVAER MDVHAVWAGW GHASENPRLP ESLAASPKKI IFIGPPASAM RSLGDKISST
IVAQHAEVPC IPWSGTGVDE VVVDDAGIVT VKDDVYSRGC TFSPEEGLTK AKEIGFPVMV
KASEGGGGKG IRKVEREEDF INLYNAAANE IPGSPIFIMK LAGNARHLEV QLLADQYGNN
ISLFGRDCSV QRRHQKIIEE APATIANPDT FQSMERAAVS LGKLVGYVSA GTVEYLYSHA
DDKFYFLELN PRLQVEHPTT EMVTGVNLPA AQLQIAMGIP LHRIRDIRLL YGVDPNTSAA
IDFDFSKEGS AETQRRPQPK GHTTACRITS EDPGEGFKPS SGTMHELNFR SSSNVWGYFS
VGTSGGIHSF SDSQFGHIFA YGENRSASRK HMVIALKELS IRGDFRTTIE YLIKLLETPA
FEENKITTGW LDQLISNKLT AERPDTTIAV LCGAVAKAHQ ASESRLTEYR QGITKGQVPP
KDVLKTVFPV DFIYEGKRYK FTATRAGLDG YHLFINGSKC SVGVRALADG GLLVLLNGRS
HNVYWKEDAA ATRLSVDGKT CLLEQENDPT QLRSPSPGKL VKFTVENGEH VSANQPYAEV
EVMKMYMPLI AQEDGIVQLI KQPGATLEAG DILGILALDD PSRIKHAQPF TEQLPPIGPP
QVVGNKPAQR FLLLHGILEN ILRGFDNQVI MNTTLKDLIG VLRDPELPYS EWNAQSSALH
SRMPSKLDNQ LQQTVDRARS RKAEFPAKQL QKTMARFIEE NVNPADADIL KTTLSPLTQV
IHDYIEGLKV HEYNVFVGLL EQYVAVEKLF SGPKSRYEDG ILALREEHKD DVEPLLQIAL
SHSRIGAKND LILAILSIYR PNQPEMGNVG QYFKGVLKRL TEIESRAAAK VTLKAREVLI
QSALPSLEER LSQMELILRS SVAESAYGES GLRHREPDFA ALKEVVDSKY TVFDVLPRFF
VHKDAWVTLA ALEVYVRRAY RAYTIQSMDY HHNGEPAFMS WDFTMGKLGQ PEFGPLTSGT
HPSTPSTPTT ESNPFRRINS ISDMSNLLND SPNDTPRKGV ILPVEYLEDA EEYLAKALEV
FPKKKHGDHG LIAALEGKRR PSARVETDSA ELTGVLNVAI RDVEDLEDTQ IVAQISKLIS
RFKEELLSRR VRRVTFICGR NGVYPSYYTF RGPSYEEDES IRHSEPALAF QLELNRLSKF
KIKPVFTENR NIHVYEAIGK GPENDKALDK RYFVRAVVRP GRLRDDIPTA EYLISEADRL
MNDILDALEV IGNNNSDLNH IFINFSPVFN LQPHDVEEAL AGFLDRFGLR LWRLRVTGAE
IRILCTDPTT QTAYPLRVII SNTVGYIIQV ELYIEKKSEK GEWLLHSIGG TNKLGANHLR
PVATPYPTKE WLQPKRYKAH VMGTQYVYDF PELFREAFQN SWAKAIAKTP SLTERRPPVG
ECMEYSELVL DDADNLVEIS RGPGTNTHGM VGWLVTARTP EYPAGRRFII VANDITFQIG
SFGPLEDKFF HKCTELARKL GIPRIYLSAN SGARIGMAEE LIPYFSVAWN NPDKPEAGFK
YLYLTPEVKE QFDASQKKDV VTELIHDDGE DRHKITTIIG AKDGLGVECL KGSGLIAGAT
SRAYEDIFTI TLVTCRSVGI GAYLVRLGQR AIQVEGQPII LTGAPAINKL LGREVYTSNL
QLGGTQIMYR NGVSHMTAAN DFDGVSKIVD WLSFVPEKKG ALPPIRSFSD TWDRDVAYYP
PPKQPYDVRW LINGKQDDEG FLPGIFDTGS FEEALGGWAR TVVVGRARLG GIPMGVIAVE
TRPVENVTPA DPANPDSMEM IAQEAGGVWY PNSSFKTAQA LRDFNNGEQL PVMILANWRG
FSGGQRDMFN EVLKYGSYIV DALVKYEQPI FVYIPPFGEL RGGSWVVVDP TINPEQMEMY
ADEESRGGVL EPEGIVNIKF RREKQLETMA RLDPTYGELR RAAQDKNISK EKLSEIKDKM
AAREEQLLPV YMQVALQFAD LHDRAGRMKA KNTIRQSLTL KDARRFFYWR VRRRISEEAI
LKRMLRAAPS PIEGEPSGAI AKDSTPASSN DSPRDTHLRT LQSWTPFSEE ESENNDQGVA
TWYEDNKEII HEKIESLKSQ SLASHISDLL FNNRNSSLRG IQQALSMLPV EEKESVLKYL
GSN
//
