ID A0A0D0E8K1_9AGAM Unreviewed; 2189 AA.
AC A0A0D0E8K1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIK95000.1};
GN ORFNames=PAXRUDRAFT_413240 {ECO:0000313|EMBL:KIK95000.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK95000.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK95000.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK95000.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN825071; KIK95000.1; -; Genomic_DNA.
DR STRING; 930991.A0A0D0E8K1; -.
DR HOGENOM; CLU_000395_5_1_1; -.
DR InParanoid; A0A0D0E8K1; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000054538; 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; 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:UP000054538}.
FT DOMAIN 3..511
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 160..352
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 638..712
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1437..1775
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1779..2093
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 2007..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2013..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2189 AA; 242912 MW; 2A69F645BB39C378 CRC64;
MWLSTQVLIA NNGIAAVKEI RSIRQWSYET FGRERAIEFT VMATPEDLKV NAEYIRMADQ
YIEVPGGSNN NNYANVDLIV DVAERVGVHA VWAGWGHASE NPRLPESLAA CKNRIVFIGP
PGSAMRSLGD KISSTIVAQS AEVPTMAWSG SGISDTELSK QGFVTVPDKA YKNACVTSVE
EGLAKAEQIG WPVMIKASEG GGGKGIRKVD HADAFKNAYH AVAGEIPGSP IFIMKLAGQA
RHLEVQLLAD QYGNAISLFG RDCSVQRRHQ KIIEEAPVTI AKEDTFEQME RAAVRLAKLV
GYVSAGTVEY LYSHLEDVFY FLELNPRLQV EHPTTEMVSG VNLPAAQLQV AMGIPLHRIR
HIRTLYGVAP NAASEIDFDM VKPGSNQLQR KPRPKGHVVA VRITAENPDA GFKPSSGSLQ
ELNFRSSNNV WGYFSVSSAG GLHEFADSQF GHIFAYGEDR NESRKNMIVA LKELSIRGDF
RTTVEYLIKL LELEAFTENT FTTGWLDSLI SNKLTAERPD ATLAVVCGAA TKAHLAAEAC
LGEYKRILDK GQVPVRDLLK TVFSVDFIYE NIKYNFTCTR SSKNMWTLFL NGGRTMVGAR
PLADGGLLVL LDGRSHSVYW REEVGALRLM VDSKTCLIEQ ENDPTQLRSP SPGKLIRFLV
DSGDHINAGE QYAEIEVMKM YMPLVASEDG IVQFVKQPGV SLEPGDILGI LTLDDPARVK
HAKPFEGLLP PMGLPGIVGN KTYQRFVRCV GTLNDILEGY DNQAIMASTF KDLVEVLHDP
GLPYSEVSAI LSTLSGRMPS KLEEGIRTAI DAAKSKGDAQ EFPAIRIKKV LEHYVQDSIL
PQDRTMFRAQ LAPLFYVLEK FMGGLKGHEV YTLADLLSAY ESTEKLFGGS IEARVLNLRE
QHKDDLDKVV ALVLSHTKAQ SKSKLVLSIL DYVKTSGLPV SNAESRLYQV LSNLAALESK
SSTAVSLKAR EVLILGQMPS YEERLVQMEA ILKSAVTSSV YGEQGAANRT PSAEILGELS
DSRYTVYDVL PAFFSHVDPL VTLAAFEVYV RRAYRAYSLL SIDYEEGDGP DDGELPSAVT
WRFNLGRSHS PPATPSVTAP DPRRQGSVSD LTYLINRNQS QPIRTGVIAS FSDLPALSQG
FEQTAALLPV FDVNEFRHRY GSSEPPNVMN LALRIFDKAN DISEEAWAEQ ALEFVNERNA
TLVKRGVRRV TIIICKRGQY PMYFTMRGAN GVWVEEQAIR NIEPALAFQL DLSRLSNYKL
TPVFVETKQI HIYHAVAREN QLDNRFFVRA LVRPGRLRGS VSTKEYLISE TDRLVTSVLD
ALEVVSAQHR NADVNHIFMN FVYTLQVSYE DVLEAISGFI ERHGKRLWRL HVTGSEIRIA
LEDQEGNVTP IRCIIENVSG FVVNFHGYQE ITTDKGTTIL KSIGEKGPLH LQPVNQAYPT
KESLQPKRYQ AHLIGTTYVY DFPELFSKAL HNVWIKARGY DSSLNFPKTF LNAKELVLDE
HDQVTEVERA PGSNTFGMVA WVFTLRTPEF PDGRKVVVIA NDITYKIGSF GPIEDQFFYL
VTKYARAHGL PRIYLSANSG ARIGLAEEIM DLFLCAWNDD AHPEKGFEYL YLTRENYLKV
QEKAPSAIRT AEIEVNGEVR YKVTDIIGLQ DGLGVESLKG SGLIAGETSR AYDDIFTITL
VSARSVGIGA YLVRLGERAV QVEGQPIILT GAPALNKVLG REVYTSNLQL GGTQIMHKNG
VSHLTAASDL EGVTHILQWL SYIPEVKGDP LPVIETLDTW DREIAYVPPK GPYDPRWFIE
GKVDEQTSGW LSGFFDKGSF QETLSGWAQT VVVGRARLGG IPTGVIAVET RTIERVVPAD
PANPASFEQK VMEAGQVWYP NSAYKTAQAI FDFNREGLPL IIFANWRGFS GGQQDMYDEV
LKQGSKIVDG LSSYKQPVFV YIVPNGELRG GAWVVLDPSI NSSKMEMYAD VEARAGVLEP
EGIVEIKMRR DKILTLMERL DSPYASLKAA SKDPSRSAEE RAEASEALAD RETLLQPTYK
QIALLYADLH DRTGRMEAKG CAKPAVWKEA RRFFYWALRA RIARSEALNQ LTDSNPETTP
ELLEKLLNSL ISVTDPSDNR AVAAALEDLD LTSTLVKLRT DYLLQRFLEV AQQDRKASID
GLVRLVDLLS YDEKQALQSS LQNSRSPGL
//
