ID U4L322_PYROM Unreviewed; 1165 AA.
AC U4L322;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=PCON_10461 {ECO:0000313|EMBL:CCX10867.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX10867.1};
RN [1] {ECO:0000313|EMBL:CCX10867.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX10867.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX10867.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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; HF935572; CCX10867.1; -; Genomic_DNA.
DR AlphaFoldDB; U4L322; -.
DR STRING; 1076935.U4L322; -.
DR eggNOG; KOG0370; Eukaryota.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000018144; 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; -; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 218..410
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 754..950
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1017..1165
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1165 AA; 127669 MW; DC03B46BDB33A43A CRC64;
MATSLPRRFA ISPAALRPAR SFLPQNRGLS SLSKLIPKTQ TINSAKPSPA QRLASVTQAR
TFTSSRKLFD APSSKTYLAS GAIASGRDLV DVNKVLVIGS GGLSIGQAGE FDYSGSQAIK
ALKEAGKQSI LINPNIATIQ TSHFLADEVY YLPVTPEYVT HVIERERPDG ILLTFGGQTA
LNVGVQMNKM GVFDRLGVKV LGTPISTLET SEDRDLFAKA LKEIDIPIAE SVAVNTVEEA
LEAAEVVGYP VIVRSAYALG GLGSGFANNR KELHDLSAQS LSLAPQILVE KSLKGWKEVE
YEVVRDAANN CITVCNMENF DPLGVHTGDS IVVAPSQTLS DEEYHMLRSA AIKIVRHLGV
VGECNVQYAL QPDGLDYRVI EVNARLSRSS ALASKATGYP LAYTAAKIAL GHTLPELPNA
VTKTTTANFE PSLDYIVTKI PRWDLSKFQN VRRDIGSAMK SVGEVMAIGR TFEESIQKAI
RQVDPQYLGF QGAKFDDLDD VLRNPTDRRW LAVGQAMLHE GYSVEKIHEI SRIDKWFLYK
LENIVEMYKK LQQVGSLFGL NSELLLSAKK MGFSDKQIAM SVGCTEDEVR ARRKTFNIHP
WVKRIDTLAA EFPAETNYLY TTYNATEHDV KFEDNGVVIL GSGVYRIGSS VEFDWCAVSA
TLALREMGIK TVMVNYNPET YSTDFDTADK LYFEELSYER VKDIYELENS SGVVVSVGGQ
LPQNIALKLK QSGAKVLGTD PEDIDRAEDR HKFSQILDSI GVDQPAWAEL TSVSEARTFA
DKVGYPVLVR PSYVLSGAAM SVIRSESELE NKLNNASSVS PDHPVVISKF IDGAMEIDVD
AVASNGSLIL HAVSEHVENA GVHSGDATLI LPPATLDESI MARVKEIAEK VAKAWKITGP
FNMQVIKEEQ ADGSIALKVI ECNLRASRSF PFVSKVLGTN FVDVATKALV GRAPEAVDLM
KVKRDYTAIK VPQFSWTRLA GADPFLGVEM SSTGEVACFG KDVVEAYWAA IQSTMNFKVP
QPGSGILIGG NTQKPEIKKI MEYLNPMGYK LFATSQKTAS ELEALADGAK VNVLDFPKED
KRKLRDVFEG NDIKGVFNLA DKRAEDLLDV DYVMRRNAVD FNVPLFMEPK TAQLFAQCLS
EKLPLAEGTP AEVRRWSEFI GGKPL
//
