ID G0S0B3_CHATD Unreviewed; 1314 AA.
AC G0S0B3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Carbamoyl-phosphate synthase arginine-specific large chain-like protein {ECO:0000313|EMBL:EGS23274.1};
GN ORFNames=CTHT_0009410 {ECO:0000313|EMBL:EGS23274.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23274.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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};
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DR EMBL; GL988037; EGS23274.1; -; Genomic_DNA.
DR RefSeq; XP_006691465.1; XM_006691402.1.
DR STRING; 759272.G0S0B3; -.
DR GeneID; 18254979; -.
DR KEGG; cthr:CTHT_0009410; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 3.
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; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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 PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 3.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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:UP000008066};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 217..409
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 900..1097
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1165..1314
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1314 AA; 145208 MW; 8F01A0CEF7B48D4A CRC64;
MLSAVYKAGR APAVLRHGRR VPVASSQLRP LVTGSNASPF RTQADAAISS RLPQRRLLSA
TAAMAAVAQQ APNPKAYLES GVIKPKEHVD VKKVLVIGSG GLSIGQAGEF DYSGSQALKA
LKEAGVKSVL INPNIATIQT NHSLADEVYY LPVTPEYVEY VIQKEKPDGI FLSFGGQTAL
NLGVQMQKRG LFEKYGVRVL GTSIRTLELS EDRDLFAKAL EEINIPIAKS IAVNTVDEAL
EAARKVGYPI IVRAAYALGG LGSGFANNEE ELRNMAARSL TLSPQILVEK SLKGWKEVEY
EVVRDANNNC ITVCNMENFD PLGIHTGDSI VVAPSQTLSD EEYHMLRSAA IKIVRHLGVV
GECNVQYALQ PDGLDYRVIE VNARLSRSSA LASKATGYPL AYTAAKIGLG HSLPELPNAV
TKTTTANFEP SLDYIVTKIP RWDLSKFQHV KRDIGSAMKS VGEVMAIGRT FEESFQKAIR
MVDPKFVGFQ GAKFEDLDYE LQNPTDRRWL AIGQAMLHEN YTVDRIHELT KIDKWFLYKL
QNIVDCTKEL QQIGSLSALK KEHILKAKKL GFSDKQIAIA VGSTEDEVRA RRLEFGIRPW
VKKIDTLAAE FPADTNYLYT TYNASSHDVT FDDKGTIVLG SGVYRIGSSV EFDWCAVSAT
QALRKIGEKT VVINQNLNTT LDVAAEASEK AQIEVKRQWN RKWHRHQLAT HREAYISALR
ECVRPPRANN PGQSAARARE RAQRAFGEVL LQPVVTKPPS TNTATRVTFG TCTRERMALP
EKQPYFCLLC KCTLASNSNW HRYRRTDRHL EHINALKKSG MNPETLSTDY DNADRLYFEE
LSYERVMDIY ELEEASGVVV SVGGQLPQNI ALRLQETGGA NVLGTDPRNI DRAEDRQKFS
EILDSIGVDQ PAWKELTSVK AAEEFAEQVG YPVLVRPSYV LSGAAMTVIR SKEELKDKLE
AAAEVSPDHP VVISKFIEGA QEIDLDAVAY QGNLILHAVS EHVEQAGVHS GDATLVLPPV
NLDNDIMQRL KDIAQKIAKA LQITGPFNMQ VIKADDPEGG APALKVIECN LRASRSFPFV
SKVLGTNFID VATKALVGKN VPEPVDLMAV KRNYLATKVP QFSWTRLAGA DPFLGVEMAS
TGEVACFGKD LVEAYWTSLQ STMNFRVPEP GEGLLFGGEL SKPWLTAVVD YLAPLGYKLY
AADAEVKKHL ESTSKHAISV QVIEFPAHDK RALREVFEKY DIRGVFNLAQ ARGKTIHDVD
YVMRRNAVDF GVPLFMEPQT AILFAQCLSE KLPRPSGIPS EVRRWSEFLG GKPL
//
