ID A0A166DD29_9AGAM Unreviewed; 2260 AA.
AC A0A166DD29;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carbamoyl-phosphate synth {ECO:0000313|EMBL:KZT38386.1};
GN ORFNames=SISSUDRAFT_1004759 {ECO:0000313|EMBL:KZT38386.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT38386.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT38386.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT38386.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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 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 ---------------------------------------------------------------------------
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; KV428064; KZT38386.1; -; Genomic_DNA.
DR STRING; 1314776.A0A166DD29; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000076798; 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:UP000076798};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 595..787
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1130..1321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1387..1543
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2260 AA; 247803 MW; 693EA63B2CD8E90F CRC64;
MSSTMKPLRP VHSRANSLFG IPNGSLTSRQ SDRNEAPDDA VLQLEDGTTV KGISFGAPGK
SVSGECVFQT GMVGYTESLT DPSYEGQILI LTYPIVGNYG VPKREVEQAI DSIPEEFESS
RIHIAGLVVG YYSEDFSHFL ANSSLGAWLK ENGIPAIYGI DTRMLTKKIR EKGTLLGKIL
ARKEVTETTS HLNSRHVSRP PSRGGSPSSG ANWLQDYIDI PLHDPNAENL VAVVSTKTPK
LFKPTSTPKL HPSGRPLRVL AIDVGMKYNQ IRCFTHRGVE LKVVPWDYNF NASTEEPYDG
LFVSNGPGDP TMVSETIENL RVALEKADRP IFGICLGHQL LALAAGATTS KMKYGNRGHN
IPCTDSFSGR CYITSQNHGF QVDTDSLPSG WSELFVNAND GSNEGIFSED KPFFSVQFHP
ESTPGPRDTE FLFDVFIQNI IDCVTTGVMA PISMPGGDIA TNERLHQRVE VSKVLVLGSG
GLSIGQAGEF DYSGSQAIKA LKEEGIYTVL VNPNIATIAT SKGLADKVYF LPVTPEFVLK
IIKYEKPDGI YVTFGGQTAL NVGIKLKDQF EALGCKVLGT PIDTIITTED RHLFATAMEE
IGERCAQSST ATTPDEAVVA AAEIGYPVIV RAAYALGGLG SGFAQDESQL RELCGKAFAT
SPQVLVEKSM KGWKEIEYEV VRDCRDNCIT VCNMENFDPL GIHTGDSIVI APSQTLSDVD
FNMLRTTAIN VIRHLGVVGE CNIQYALNPF SREYCIIEVN ARLSRSSALA SKATGYPLAF
IAAKLGLGIP LNEIRNSVTR VTSACFEPSL DYVVVKIPRW DLKKFTRVSK LLSSSMKSVG
EVMSIGRTFE ETIQKAIRAI DDSFTGFAKN DLVDDIDEEL TNPTDKRMFA ISTAFHRGYS
VEQVWKLTNI DKWFLTKLHH IFKMECALSK SSLSSLSSYT LLRAKQMGFS DRQLATCLGS
TELAVRRLRQ EHGIAPFVKQ IDTVAAEFPA FTNYLYTSYN ASEHDVDFED RGVMVLGSGV
YRIGSSVEFD WCAVRAIRTL REQGLKTIMV NYNPETVSTD YDEADRLYFE NISLETILDI
YDAERARGVI LSMGGQTPNN IALPLHRQNV KIYGTSPEMI DTAENRYKFS RLLDKIGVDQ
PTWKELTSFE EAQNFCDKVE YPVLVRPSYV LSGAAMNVVY TPDDLHNYLT QATAVSRDHP
VVITKYIEGA KEIEMDAVAR DGKLMMHYIS EHVENAGIHS GDATLILPPQ DLDPETVRRI
EDATAKIGNA LNVTGPFNIQ FIAKNNDIKV IECNLRAARS FPFVSKVTGV DAIEMATKVM
LGLRVEPYPE LSLPPDYVGV KVPQFSFSRL SGADPVLGVE MASTGEVACF GKDKYEAYLK
ALLSTGIVLP KKNILLSIGG FKEKLEILPS VQKLRAAGFN IFATAGTADF LVEHNVPCKY
LETLGEEGAD KQKSEYSLTE HLAKHLIDMY INLPSKNHYR RPASYTSKGY RTRRLAVDFA
VPLITNVKCA KLLIEALVRK MPLDVSPIDF KTSHTTYTFP GLVNISSFVP GLLERGSRDF
NDATRASLGG GFTTALILPS SVNGELTDSE TLDTAHSNAT GACHCDYALS ITATDKNIAN
ITESVHSQCK ALYLSPSSAS GFGTALGTIA SHFSSWPTEK PIIVTANGSD TASALLLASL
HNRSVHVANV RTKEDILLVA LSKTKDLRVT CDVSVYSLFF TKEEYSDAPC LPSALDQKIL
WESMGVIDAF SIGRTPYDLA EHLGKPASAW SGVEEALPLL LNAASEGRLT LRDIQERLHD
NPARIFGLTE QGLTQVEVVV DRKAAFVPSH RSWSPLSRKS LTGAVHRVVI HGQTVLLDRA
LFSSPIGRDV SSTVVAPRLA GERSSRASFS SSIRPTISTL TEVSSPPAAA ALKSPTAVTL
DIGSTQPIPL SLSHSTIQQI ASSTSRSFPL PPPHPAFHRR HILSIKQFTH QDIHDLFSLA
HEMRLQVERN GTLDILKGRV LCTLFYEPST RTSASFEAAM KRLGGEVVSV SATHSSVQKG
ESLADTVRTL GCYGDAIVLR HPEIGSPQTA AKFSPVPILN AGDGVGEHPT QALLDVYTIR
SELGTVNGRT ITLLGDLKNG RTVHSLVSAL CLYSVTLNFV APPGLEMPER VVTAARRAGV
HVRQCESLEE VLADTDVLYV TRVQRERFEN PEEWERVKNS YVVNHAVLSR AKEDMIVMHP
LPRVNEIDPD VDFDSRRAVY FRQMRYGLFV RMALLASVMA
//
