ID A0A137P6F3_CONC2 Unreviewed; 1147 AA.
AC A0A137P6F3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=CONCODRAFT_39342 {ECO:0000313|EMBL:KXN70539.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN70539.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN70539.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN70539.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KQ964499; KXN70539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137P6F3; -.
DR STRING; 796925.A0A137P6F3; -.
DR EnsemblFungi; KXN70539; KXN70539; CONCODRAFT_39342.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000070444; 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 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 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; 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; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
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:UP000070444};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 148..340
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 703..900
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1147 AA; 127060 MW; 3650A6ED9BC35DD5 CRC64;
MSTSIPNNID TINYTTLEKP SYEKVLVVGS GGLSIGQAGE FDYSGSQAIK ALKENGIKTV
LVNPNIATIQ TGQELADEVY FSPVTPEFLE EVIQKERPDG IFLSFGGQTA LNCGIELYNR
GILEKYQVKV LGTPIQTLIT SEDRDLFVKA LNEINIPVAQ STAVSTVEDA LKAAEEIGYP
IIIRSAFSLG GLGSGFANDP EELTSLASKS LSLSPQILVE KSMKGWKEVE YEVVRDAADN
CITVCNMENF DPLGIHTGDS IVVAPSQTLS DEEYHLLRTA AIAIVRHMGV VGECNVQYAL
DPYSLEYKVI EMNARLSRSS ALASKATGYP LAFVAAKLGL GYTLPELKNS VTKTTTACFE
PSLDYVVTKI PRWDLTKFSQ VDRHVGSSMK SVGEVMAVGR TFEESLQKAI RMVDPSFLGF
HPMKNLYKSI TDKSLEKADD PVLNEFLSNP TDRRLFGVIN AMVENGYDVE KIHSLTKIDR
WFLYKLENLY KVYNQLSQHT IHTLPKDLMD QAKKSGFSDL QIAHKLSKPN AAVNELDVRQ
LRKSYGIIPL VKRIDTLAAE FPAHTNYLYT TYNASQDDIE FNDKGTMVLG SGVYRIGSSV
EFDWCGVSCI RALRKMGHKT VMLNYNPETV STDFDECDRL YFDELSLERV LDIYEREQAE
GVIVSVGGQL PQNIALPLHN IGANVLGTSP VKIDQAEDRY KFSKTLDEIG VDQPAWKELT
TTEQAFEFAN QVGYPVLVRP SYVLSGAAMN VAHTEEDLNR FLSLATDVSP LHPVVVTKFE
QNSQEIDVDC VAQKGNVLCH AISEHIEPAG VHSGDATLVL PPKDLPQQTK DNIYEIAKKV
AKAFDITGPF NMQIIRKEGS QSSEEQLKVI ECNLRASRSF PFVSKVLNHN FIDTAAQAMT
QKEDVKPVNL MDKEYPYQAV KASQFSWTRL QGADPFLGVE MASTGEVACF GKDKHEAYLA
AIQSTTGFKL PKQAVLISSG DDHAPLKVVT RVANLIKEVA NLEVVVWNQY IYDAIKAKLP
ELEIKLISFP SLADVQNPLH LNNQIRDVLK ENGVDMVMDF SRDKPIGAPS IQQLVEQKKK
SNGVGEDNSY LGYLIRRSAV DIGIPLINQS NLSTLFAEAI SKYPIDSDGK PNVEVNGWNH
YLEQLKE
//
