ID A0A316Z6M0_9BASI Unreviewed; 2315 AA.
AC A0A316Z6M0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative URA2-multifunctional pyrimidine biosynthesis protein {ECO:0000313|EMBL:PWN96602.1};
GN ORFNames=FA09DRAFT_331096 {ECO:0000313|EMBL:PWN96602.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN96602.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWN96602.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN96602.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001363};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004812}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004852}.
CC -!- SIMILARITY: In the 2nd section; belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00043998}.
CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily.
CC {ECO:0000256|ARBA:ARBA00043968}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
CC {ECO:0000256|ARBA:ARBA00043979}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00043984}.
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DR EMBL; KZ819298; PWN96602.1; -; Genomic_DNA.
DR STRING; 58919.A0A316Z6M0; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000245946; Unassembled WGS sequence.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR00670; asp_carb_tr; 1.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000245946};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 613..805
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1150..1341
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1408..1569
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2315 AA; 249932 MW; 19BA09A6CCDCCC4F CRC64;
MSSSTSASAA AAAPARPAPM VRSATVQRTP SPAPPATSAP LGSAPAPSML LELADGSAHR
GISFGAEGKS ISGECVFQTG MVGYVESLTD PSYEGQILVL TFPLAGNYGV PSREEAESSI
ASLLASPFES SRIHVAGLVV AYYSHDFAHY LAASSLGAWL KEQGVPAIYG VDTRALTKRI
RSSGSMLGKL LAARSAPAPA NGVAADWRAE FDDVPYADPN ARNLVAVVSS TQPRLYTPAN
TSAGGSLAPA GVAPLQHPSG RPLRILALDV GMKYNQIRCF TSRGAELKVV PWDHDFLAAS
EEPFDGLFIS NGPGDPTSCA PTIARIAKLM ERTGVAAIPI FGICLGHQLL ALAAGAKTEK
MKFGNRGHNI PCTDQLSGRC YITSQNHGYQ VLASSLPAHK GWGELFVNAN DGSNEGIHCT
QGPYFSVQFH PESTPGPRDT EFLFDVFLRS VQDCAAIKAA GDDAAQLPPV AFTGGLAAEN
AAVYPRVDVR KVLVLGSGGL SIGQAGEFDY SGSQAIKALK EEGIYTVLIN PNIATIQTSA
GLADKVYFLP VTPEFVLKTV RHERPDGIYV TFGGQTALNV GIAIKEELEK LGVKILGTPI
DTIITTEDRE LFARAMEQIG ERCAPSASAV NWDEALAASK SIGFPVIVRA AFALGGLGSG
FAKNEEELRR LCVAAFANSP QVLVEKSMKG WKEVEYEVVR DCRNNCITVC NMENFDPLGI
HTGDSIVIAP SQTLDDADYN MLRTTAVNVI RHLGVVGECN IQYALNPHSK EYCIIEVNAR
LSRSSALASK ATGYPLAFIA AKLGLGIPLN EIRNSVTRET SACFEPSLDY VVCKFPRWDL
RKFVRVSSKL GSSMKSVGEV MSIGRTFEEA IQKAIRSIDY QFDGFGQNDY ADPAEIDEEL
MNPTDKRMFA IANAFAKGYT VDQIHQASSI DRWFLSKLKG LSDAAEVFRT YTAGTLPVAL
LTQAKQLGFS DRQMAKFLSS TELAVRSMRK EHNIMPFVKQ IDTVAAEFPA YTNYLYTTYN
AAEHDVKFED KGVMVLGSGV YRIGSSVEFD WCAVRAIRTL RERGFKTVMV NYNPETVSTD
YDEADRLYFE NISLETVMDI YDAERATGVI ISMGGQTPNN IALPLHRQNV KILGTSPEMI
DMAENRYKFS RMLDKIGVDQ PLWKELTSFE EAHEACARFG YPVLVRPSYV LSGAAMNVVY
SPEDLSSYLS QATAVNRDHP VVITKYLEGA KEIEMDAVAR DGKMIMHYVS EHVENAGVHS
GDATLILPPQ DLDPETVRRI EAATAKIAAS LHVTGPFNIQ FIAKNNEIKV IECNVRAARS
FPFVSKVTGV DAIQMATDVM LGLPVEPYPP LQMPSRDYVG VKVPQFSFSR LAGADPILGV
EMASTGEVAC MGRNKYEAYL KGMIASGIKL PTKNVLLSIG SFSEKVELLP SVRTLHALGF
TLYGSSGSAD FYSEHGVPVI HLEALPEDDE WKGEESSKAA YSLLTHLDQG LSSLFISLPS
KNKYRRPVNF TSMGYRARRL AIDRSIPLIT NVKNAKLFVE AIARHRAAGS NFDISPVDFK
TSHTSHTFPG LVNVQAFVPS LADPATGARD IAAITKASLA AGFTTVQFMP VGLKAGHAIT
DEGSLAVAEG KVSGSAHCDV ALSLSATREN SALVAELAQR ARSLVVSFDA LGADVSKIAT
LSAHFAAWPE SRPIVTDARG NDLASVLLLA SLHSRSVHVT NVMRRDDMAL VVLSKAKGMD
VTCDVGVYSL FFNTEMYPQA SCLPSADDQA ALWEHMVDID VFCVGATPYR LALELGETPA
PEAGIQETMR LLLEAVNEQR LTLDDVLTRL STRPREIFRI AEQPDTHIEV DVDRPAVLRR
QAHWSPLSAR STRGFIHRVL VRGKAVVVDG ESLSDGTFGA NIAGVLTAAT SSKAIAVATP
GVQAAAAARR VSFSQTPGTS SQRPVLPFDV PSSPPQLALG DAKSPQLGSL EVIAPPAAQR
QSVSLMSAFA PSPAAAPDAR LPSLRSMLVH PTYTRKHILT PRQFNRDDLH ALFTVAQELR
LQVERHGVID VLRGRVLTTL FFEESTRTSC SFEAAMVRGG GQVVAVNTSR SSVSKGESLA
DTIRTVGAYT DAVVLRHPQI GSAQEAAKAS PVPVINAGDG AGDHPTQALL DVFTIREELG
TVSGLTVTLL GDLRYGRTTH SLVELLALYG VTLNFVAPAG LEMPEAIKRS LSKKGIRQYE
TSNIEEVISS TDVLYVTRTQ KERFASPEAY EAVKGSYRVD QRLLSRAKPT MVLLHPLPRN
DELADDVMYD DRCAVFRQVK AGLYVRLALL AMVLA
//
