ID G0RMB1_HYPJQ Unreviewed; 1162 AA.
AC G0RMB1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Ammonium-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044318};
DE EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE AltName: Full=Arginine-specific carbamoyl phosphate synthetase, ammonia chain {ECO:0000256|ARBA:ARBA00044249};
DE AltName: Full=Glutamine-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044334};
GN ORFNames=TRIREDRAFT_108459 {ECO:0000313|EMBL:EGR47768.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR47768.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR47768.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000256|ARBA:ARBA00044031}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; GL985067; EGR47768.1; -; Genomic_DNA.
DR RefSeq; XP_006966384.1; XM_006966322.1.
DR AlphaFoldDB; G0RMB1; -.
DR STRING; 431241.G0RMB1; -.
DR EnsemblFungi; EGR47768; EGR47768; TRIREDRAFT_108459.
DR GeneID; 18481675; -.
DR KEGG; tre:TRIREDRAFT_108459; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_108459; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 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; 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; IPR006275; CarbamoylP_synth_lsu.
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 NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 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; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 211..403
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 748..945
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1013..1162
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1162 AA; 127587 MW; E673E9D8AF944B25 CRC64;
MSSAALAAAR APALLRSGAR LPRTLPTRLF TTAALRTQAR ASLPAKAPKR LGTISVFRPY
SSTTQAAPNP KAYLDSGVIK PKVNVDVKKV LVIGSGGLAI GQAGEFDYSG AQALKALKEA
GVASVLINPN IATIQTNHSL ADEVYYLPVT PEYVSYVIER ERPDGIYLSG QTALNLGVQM
QRLGLFEKYG VKVLGTSVRT LEVSEDRDLF AKALEEINIP IAKSIAVNTV DEALDAASKI
GYPIIVRAAY ALGGLGSGFA NNEEELRNMA ARSLTLSPQI LVEKSLKGWK EVEYEVVRDA
NNNCITVCNM ENFDPLGIHT GDSIVVAPSQ TLSDEEYHML RTAAIKIVRH LGVVGECNVQ
YALQPDGLDY RVIEVNARLS RSSALASKAT GYPLAYTAAK IGLGHSLPEL PNAVTKTTTA
NFEPSLDYIV TKIPRWDLSK FQHVKRDIGS AMKSVGEVMA IGRTFEESFQ KAIRQVDPKF
VGFQGDKFED LDYELQNPTD RRWLAVGQAM LHENYSVDKV HELTKIDKWF LYKLQNLVDC
TRELEAAGSL DALQKEQILK AKKMGFSDKQ IANAVNSTED EVRARRRSFN IHPWVKKIDT
LAAEFPADTN YLYTTYNGSS HDVTFDDKGT IILGSGVYRI GSSVEFDWCA VGATQALRKL
GEKTIMINYN PETMSTDYDS ADRLYFDELS YERVMDIYEL EAAQGVVVSV GGQLPQNIAL
RLQEAGGAKV LGTDPKDIDK AEDRQKFSEI LDSIGVDQPA WKELTSVEEA AQFAEQVGYP
VLVRPSYVLS GAAMTVIRSK EDLKEKLEAA ADVSPDHPVV ITKFIEGAQE IDVDGVASQG
NLILHAVSEH VEQAGVHSGD ATLVLPPVNL DASTMERLKE IAQKVAKAWK ITGPFNMQII
KADNPEGGEP LLKVIECNLR ASRSFPFVSK VLGTNFIDVA TKALVGKDVP EPTDVMTVKR
DYVATKVPQF SWTRLAGADP FLGVEMASTG EIACFGKDLV DAYWTSLQST MNFRVPEPGE
GLLFGGELNK PWLTQVVDYL APLGYTLYAA SNDVKKFIES SSKHNVKVEV IEFPTDDKRA
LREVFKKYDI RGVFNLALAR GKTTQDVDYV MRRNAVDFGV PLFMEPQTAI LFAQCMSEKL
PRPEGIPSEV RAWSEFIGGK PL
//