ID A0A8H7RBU1_9FUNG Unreviewed; 2249 AA. AC A0A8H7RBU1; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 27-MAR-2024, entry version 9. DE RecName: Full=Aspartate carbamoyltransferase {ECO:0008006|Google:ProtNLM}; GN ORFNames=INT47_006157 {ECO:0000313|EMBL:KAG2208301.1}; OS Mucor saturninus. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina; OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor. OX NCBI_TaxID=64648 {ECO:0000313|EMBL:KAG2208301.1, ECO:0000313|Proteomes:UP000603453}; RN [1] {ECO:0000313|EMBL:KAG2208301.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WA0000017839 {ECO:0000313|EMBL:KAG2208301.1}; RA Muszewska A., Okrasinska A., Steczkiewicz K., Drgas O., Orlowska M., RA Perlinska-Lenart U., Aleksandrzak-Piekarczyk T., Szatraj K., RA Zielenkiewicz U., Pilsyk S., Malc E., Mieczkowski P., Kruszewska J.S., RA Biernat P., Pawlowska J.; RT "Metabolic potential, ecology and presence of endohyphal bacteria is RT reflected in genomic diversity of Mucoromycotina."; RL Submitted (DEC-2020) 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:KAG2208301.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAEPRD010000020; KAG2208301.1; -; Genomic_DNA. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000603453; Unassembled WGS sequence. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; 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; 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:UP000603453}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 609..801 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 1146..1337 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 1403..1568 FT /note="MGS-like" FT /evidence="ECO:0000259|PROSITE:PS51855" FT REGION 1877..1900 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 349 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 433 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 435 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" SQ SEQUENCE 2249 AA; 247335 MW; 0FBAEECDC4C285CF CRC64; MVSNIPVPTI NGIAPMVLAA HITAPAANAT PIARSPRSPT APHRPAAALE DPKDVTTAAF VLKDGTSFQG ISFGSETQSI SGECVFQTGM VGYPESLTDP SYRGQILVVT FPLVGNYGVP SRTEMDELLT DLPKRFESNQ IHVAGLIVGS YATDYSHYLA ESSLATWLKE NNVPALYGID TRAMTKKIRD QGVTLAKILF PKKSAGNGLD HAALGLSIQD DGLERWMNDY ETVEWVDPNE RNLVAEVSIK EPKVYYPDPK NAIKTPSGRT MRVIAVDIGM KYNQIRCFVY RGVELKVVPW DYDFNAEPVD SYDGLFLSNG PGDPTTIELT ISRVRTYIQN IKKPIFGICL GHQVMALASG AKTIKMKYGN RGHNIPCTNM ISGRCYITSQ NHGYAVDAST LPENFSELFV NANDGSNEGL IHEKLPIFSV QFHPESTPGP RDTEFLFDVF IQNIKECLNT KSLVPVQMPG GTKAENIKKN PRVHVEKVLV LGSGGLSIGQ AGEFDYSGSQ AIKALKEEGI YTVLINPNIA TIQTSKGLAD KVYFLPVTPE FVRKVIEFEK PDGIYVTFGG QTALSVGIAL KDEFEALGVK VLGTQIDTVI TTEDRDLFAQ ALYEIDEKCA PSASAVTVEE SITAANNIGY PVIVRAAYAL GGLGSGFADN DKELIALCNK AFATSPQVLI EKSMKGWKEI EYEVVRDCQD NCITVCNMEN FDPLGIHTGD SIVVAPSQTL SDEDYNMLRT TAVNVIRHLG VVGECNIQYA LNPFSKEYCI IEVNARLSRS SALASKATGY PLAFVAAKLG LGIPLNEIKN SVTKVTCACF EPSLDYVVVK IPRWDLKKFN RVSTALSSSM KSVGEVMAIG RTFEETMQKA IRAIDYNLDG FVSSDIIKDE DIEYELTHPS DQRLFAIANA MEKGYTVDRI WELTKIDKWF LNKLMRINNL GDRLTGFTKA NLPGNLIRSA KQLGFSDRQI ANRINSNELA VRRLRQEFGV TPFVKQIDTV AAEFPAFTNY LYMTYNAVEH DITFDDNGVM VLGSGVYRIG SSVEFDWCAV RAIRTLREQK IKTVMVNYNP ETVSTDYDEA DRLYFENINM ERVLDIYEIE KSSGVLMAMG GQTPNNIALP LHRQNVKVLG TSPEMIDNAE NRYKFSRMCD NIGVDQPLWK ELTSYEEAEV FCEKVGYPVL VRPSYVLSGA AMNVVSSKDD LESYLKEAAA VSRDYPVVIS KYIEDAKEIE MDAVALDGKM IMHVVSEHVE NAGVHSGDAT LILPPQDLDP ETVRKIEVAT AKIGRALNIT GPFNIQFIAK DNEIKVIECN VRAARSFPFV SKVTGIDLVE MATLAMLGLP VTPYPKIAMP KDYVGIKVPQ FSFSRLSGAD PILGVEMAST GEVACFGKDK YQAYLKALLA TGFSLPKKNI LFSIGSYKEK IEMLPSVKRL HELGYSLFAT TGTADFISEH GIPVKHLDTL DADTDDQIKA EYSLQQHLSN NMIDLYVNLP SRNRFRRPAS YMSKGYRSRR MAVDYDIPLL TNVKCAKLFV EALARKKDFE ILGIDFKSSS NTATLPGLFN INAFLPSTED LATVTNTSLK SGFTTISAVC DDVKDQASLE TMSSAAHKNA SVDYLLSITA TAENADQLDS VASEAAAVYI DTDKIGSGNV SVFDSVFDSW PSNQVMITEA KATDLASILL LASIHSRVIH VSNVTTKDDL ALIEMTKNKG LKVTCDVSIY SLFLNKSDVD SKLLPSVADQ EGLWKKLHVI DCFSVGSTPA KLDSTSNAAG IAEALPLLLT AVAQGRLTIQ DISERMNDNP RRIFGLSPQT DTYIDVELDR SKAWTTGPLA GKKTQGSISR VVVNGTTVFM DGVLRVAGSL GRDLSVQAKA AELVVPAPKK KADSTPSDAD ISDVPETAPE RKSIQPFDPI KLAGASDQQL VAFATPSYEI SASLARVVSR SPFYRKHILR SKQFDRSDLH LLFGVAHEMR NMVELYGSIN LLQGRVMSTM FFEPSTRTSC SFEAAMYRLG GKVVSVSATT SSVQKGETLS DTVRTLGCYT DLIVLRHPQP GSAQIAAKHS KVPIINAGDG IGEHPTQAFL DVFTIREELG TVNGLSITMV GDLKNGRTVH SLVKILAYYQ VTINYVCPDS LAMPKDVMEE VAAAGITQNV YASLDEVIGI TDVLYMTRVQ KERFDTEEEY RRVKDAYILN NNVLSKAKSQ MIIMHPLPRV NEIEPEVDFD QRAAYFRQMR YGLYVRMALL ALVMGTHRG //