ID A0A151GUA2_9HYPO Unreviewed; 1888 AA.
AC A0A151GUA2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Aspartate carbamoyltransferase catalytic subunit {ECO:0000313|EMBL:KYK60651.1};
GN ORFNames=DCS_01789 {ECO:0000313|EMBL:KYK60651.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK60651.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK60651.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK60651.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYK60651.1}.
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DR EMBL; LAYC01000001; KYK60651.1; -; Genomic_DNA.
DR STRING; 98403.A0A151GUA2; -.
DR InParanoid; A0A151GUA2; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000076580; Chromosome 01.
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; 3.40.50.1380; 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; 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; 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:UP000076580};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KYK60651.1}.
FT DOMAIN 567..759
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1104..1295
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1361..1519
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1510..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1888 AA; 207899 MW; D4B5ADE977C71587 CRC64;
MALQPATARM ASAHDEGRIC LELEDGSAYQ GYSFGADKSI AGELVFQTGL VGYPESLTDP
SYRGQILVIT FPLVGNYGVP SREAVDELLG DLPAHFESSQ IHVAGLVAAS YCGEDYSHFL
ATSSLGTWLK EQGVPAMYGV DTRCLTKKIR QKGSMLGKMR LEARALLNGD ASASDPLTAT
SLERFAPVDW VNPNEVNLVA QVSIKAPRLF KPPPSVAVRK HPSGRPIRVL CVDVGMKYNQ
LRCFLRRGVE VMVCPWDHDL ADEAVNQYDG LFISNGPGDP SVLAVTVKNV RAAMEKNKTP
VFGICLGHQL LARASGAQTT KMKFGNRGHN IPCTSMVTGK CHITSQNHGF AVDASSLPAG
WKELFVNAND GSNEGIMHVD KPYFSVQFHP ESTPGPRDTE FLFDVFVDTV ARCAAEPALL
RQPVSFPGGT VEENERLHPR VSVKKVLVLG SGGLSIGQAG EFDYSGSQAI KALKEEGLYT
VLINPNIATI QTSKGLADKV YFLPVNAEFV RKVIHYERPD AIYVTFGGQT ALQVGIELKD
EFEGLGVKVL GTPIETIITT EDRELFARSM ESIGEKCAKS ASANNVDEAM KAVKDIGFPV
IVRAAYALGG LGSGFANNED ELMDLCKKAF AASPQVLIER SMKGWKEIEY EVVRDAQDNC
ITVCNMENFD PLGIHTGDSI VVAPSQTLSD EDYNMLRTTA VNVIRHLGVV GECNIQYALN
PFSREYCIIE VNARLSRSSA LASKATGYPL AFIAAKLGLG IPLKEVSNSV TKVTCACFEP
SLDYVVVKMP RWDLKKFTRV STQLGSSMKS VGEVMSIGRS FEEAIQKAIR AIDFHNLGFG
ETEALVSIDD ELQTPSDQRL FAIANAMHQG YSVDKIWEMT KIDKWFLRKL SSLSEFAKDM
SRYTTKDIAR SPEIMLQAKR LGFCDRQLAN FWDSNELAVR RMRLEAGIKP FVKQIDTVAA
EFPAFTNYLY LTYNASEHDV DFNDHGVMVL GSGVYRIGSS VEFDWCSVRA IRTLRKSGFK
TIMVNYNPET VSTDYDEADK LYFENINLET VLDIYQLEAA SGVLGAMGGQ TPNNIALPLH
RAGVKVLGTS PEMIDMAENR YKFSRMLDLI EVDQPTWKEL TSFDEAREFC NTVSYPVLVR
PSYVLSGAAM NTVYSEKDLV NYLTQAAEVS RDHPVVISKY IENAKEIEMD AVAKDGVVVG
HFISEHVENA GVHSGDATLI LPPQDLEATT IQRIEEATRK IGAALNVTGP FNIQFIAKDN
DIKVIECNVR ASRSFPFVSK VMGVDLIEMA TKAIMHQPFQ AHPPTTLPPN CVGVKVPQFS
FSRLSGADPV LGVEMASTGE VACFGVDKYE AYLKALLSTG FKVPKANVLL SIGSFKDKNE
MLPSVQKLQR IGYKLFATAG TADFLQEHGV QVQFLEVLGS DEDMNSEFSL TQHLAKNTID
LYINLPSNNK YRRPANYMSK GYMTRRMAVD YQIPLVTNVK NAKLLIEAIA RHVYLDVSKR
DFQITSEPAT TGLMPSVKSP EPMPSIGQSA ADARRPVTRD GNPSVAVGGL GSPMRCVADE
LSPSTLSSIK PSVLQILSQP SIFRKSHVLS VKQYTRSDLH MLFTVAQEMR LGVQREGVLN
LLRGKVLCTL FYEPSTRTSA SFDAAMQRLG GRTVAVSTSQ SSVQKGESLQ DTLRTLACYG
DAIVLRHPDE KSVDIAEKYS DVPVINGGNG SQEHPTQAFL DLFTIREELG TVQGLTITFL
GDLLHGRPVH SLVYLLRHYQ VKVQLVAPKG LGLPEPVREQ LVSAGQLLCE SETLTSEIIA
RSDVLYCTRV QKERFESAEK YERVKDSYRV DNAALKHAKS SMVVMHPLPR NEEVADEVDF
DQRAAYFRQM RYGLYCRMAL LALVMSTS
//
