ID A0A1Y1WRZ8_9FUNG Unreviewed; 2173 AA.
AC A0A1Y1WRZ8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carbamoyl-phosphate synth {ECO:0000313|EMBL:ORX76323.1};
GN ORFNames=BCR32DRAFT_209269 {ECO:0000313|EMBL:ORX76323.1};
OS Anaeromyces robustus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Anaeromyces.
OX NCBI_TaxID=1754192 {ECO:0000313|EMBL:ORX76323.1, ECO:0000313|Proteomes:UP000193944};
RN [1] {ECO:0000313|EMBL:ORX76323.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX76323.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX76323.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX76323.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORX76323.1}.
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DR EMBL; MCFG01000306; ORX76323.1; -; Genomic_DNA.
DR STRING; 1754192.A0A1Y1WRZ8; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000193944; 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:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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; IPR011059; Metal-dep_hydrolase_composite.
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; SSF51338; Composite domain of metallo-dependent hydrolases; 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:UP000193944};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 529..721
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1064..1255
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1321..1469
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 274
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 358
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2173 AA; 242458 MW; 36F0E7362FD67C5C CRC64;
MPSAIRKSIP HPPVHAILEE NPVIGTLYLK DNTAFQGISF GAKHSIAGEC VFQTGMVGYP
ESLTDPSYRG QILVLTFPLV GNYGVPSREE VEKELNNLPK YFESSRIHVA GLIIGQYSLD
YSHYLAKSSL ADWLIENDVP ALYGIDTRAL TKKIRKQDDV EWHDPNTRNL VAEVSTKEIQ
YYKADPSKAV KGPDGKTIQI LVIDVGMKNN QIRCFVNRGV DIKVVPWDYD FLNDDDYDAV
FVSNGPGDPS SLKITIEHLR AQIKKENKPM FGICLGHQLI SLAAGATTRK MKFGNRGHNI
PCTDMKTGRC YITSQNHGYA VDVKTLPEGW KEYFVNANDA SNEGIYHETL PYFSVQFHPE
ATPGPKDTEY LFDDFISVVK ECKSAGKLVS LQKKEKVNTP KRVNIRKVLI LGSGGLSIGQ
AGEFDYSGSQ AIKAFKEEGI YTILINPNIA TIQTSQGLAD KIYFLPVTAD FVRKVIRHEK
PDGICCTFGG QTALNVGVKL KDEFEGLGVK VLGTPIETIE MTEDRELFAQ ALYEINEKCA
KSEAASSLEE AIEAANRIQY PLIIRAAYTL GGLGSGFAEN EEQLRDICNK AFATSPQVLV
ERSMKGWKEI EYEVVRDIND NCVTVCNMEN FDPLGIHTGD SIVVAPSQTL SDEDYMMLRN
TAINVVRHLG VIGECNIQYA LNPQSKEYCI IEVNARLSRS SALASKATGY PLAFVAAKLA
LGIPLTEVMN NVTKSTIACF EPSLDYCIVK IPRWDLKKFN RVSTKISSSM KSVGEVMAIG
RTFEETIQKA IRAVDDSFIG FGMDKQIPSI EDELIHPSDQ RLFAIGNAFH KGYTVDKIWE
LTRIDKWFLN KLKNIVDLEQ KIANYTTSTI PKSLLLSSKQ LGFSDVQLGK ILQTSELAIR
KLRMDYQIKP FVKQIDTVAA EFPCYTNYLY MTYNAVEHDI SFNDHGVMVL GSGVYRIGSS
VEFDWCAVRA IRTLRENHVK TIMVNYNPET VSTDYDEADR LYFETLTLER VLDIYEVESS
EGVIISMGGQ TPNNIALRLH RQNVKILGTS PEMIDNAENR YKFSRMLDKI GVDQPQWKEL
TSIDEAGKFC ESVGYPVLVR PSYVLSGAAM NVVYSENDLQ NFLEQATAVS REYPVVITKY
IEEAKEIEMD AVAVNGKLIM HVISEHVENA GVHSGDATLV LPPQDLDPET IKKLENATRK
IGNALNVTGP YNIQFIAKNN EIKVIECNVR SSRSFPFVSK VVGIDLIELA TKVMLNLPID
TEKLENVTYD RVAVKVPQFS FSRLTGADPV LGVEMASTGE VACFGDNKYE AYLKALLSTG
FTLPKKNILL SIGSYKEKVE FLPSVKRLHE MGFQLFATSG TADFIHEHGI PVKYLEAIDN
EKGPYQEYSL SQHLSNNLID LYINLPSKNR FRRPASYIST GYKTRRMAVD LAVPLITNVK
CAKLFVEALS RKFKFDISSN DFKTSHHTAQ IPGLINVQTF FNNLSKTKVD EAQDFTALTK
GAIAGGFTIS SLMPIGDECV LSNSSELQKT HNNCHGKAYC DYILNALATP TNIDEISNIV
SDTTSLLIPL NEKDPITLKD KMAEIIKFLN DWPSSFPVVA DAKNADLAAF MFLADLQDRA
IHITNVTTEQ DISLIAMSKE KGLKVTCDVN VYNLFLSNAD FDSKYLSSPS DVEALWNHIE
VIDCFSVGAT PFYVAKENGH ESTSAGIEEA LPLLLTAVND GRLTLDDIVN RLYHNPRRIF
EIPEQANTYV EIELDRKIDV VKDSFETSSL VWSALEGKTL YGHVHRTVIR GQTVYLDGAF
FPEAVKGRDL SAIVNITNTP HTPKETTLIS PPAMMTEPKS ILRAPRSQYI ADLPNSLSSI
FGGASPFYKQ HILSVRQFDR DNLHLLFGVA QEMRTVVERQ GYIPLLTGRI LCTAFYEPST
RTCSSFETAM LRLGGSVVPI KENTSSVTKG ETLQDTIRTV GMYADVIALR HKEAGAASLA
AKYSNIPIIN AGDGTGEHPT QAFLDAFTIR EELGTLNNLT ITLVGDLKNG RTVHSLCRLL
SNYQIKINYV SPESLRMPKE IIEELNTLNI PQKEFTDLNE VIADTDVLYV TRIQKERFEN
EEDYKKVFNS YVINNSVLSN AKSTMIVMHP LPRVNEISPE VDFDPRAAYF RQMKYGLYVR
MALLSLVLGK RTL
//
