ID A0A286UX96_9AGAM Unreviewed; 1165 AA.
AC A0A286UX96;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=PNOK_0130100 {ECO:0000313|EMBL:PAV24233.1};
OS Pyrrhoderma noxium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV24233.1, ECO:0000313|Proteomes:UP000217199};
RN [1] {ECO:0000313|Proteomes:UP000217199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA Kikuchi T., Tsai I.J.;
RT "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT Hymenochaetales Members.";
RL bioRxiv 0:0-0(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV24233.1}.
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DR EMBL; NBII01000001; PAV24233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286UX96; -.
DR STRING; 2282107.A0A286UX96; -.
DR InParanoid; A0A286UX96; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000217199; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 210..402
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 748..944
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1012..1165
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1165 AA; 127531 MW; 8C2EA3F9C70F2772 CRC64;
MASTRLLSKH ALTKHVGKQL GYARAFSQCI PRYALAPSAK RCAIAAPAVG SYTPKDGEHV
LNSPSELARK ISAKVLPKMP RPDVRKVVIV GSGGLSIGQA GEFDYSGSQA LKALREEGVD
AVLINPNIAT WQTSHQLASE VYFLPITADY VAYVLEKERP DGILLTFGGQ SALNVGIQLD
KMGVLDRLGV QVLGTPIRTL EVSEDRDLFV QALKEIDIPV AQSTAVSSVN AALDAAQQIG
YPVILRSAFT LGGLGSGFAN NPDELRDLAA KSLSLSPQVL IERSMKGWKE LEYEVVRDAA
DNTIICCNME NFDPLGTHTG DSIVVAPSQT LPDDEYHMLR SAALKTIRHL GVVGECNIQY
ALHPYSKEYC VIEVNARLSR SSALASKATG YPLAYTAAKI ALGHTLPELP NAVTKTTTAC
FEPSLDYIVT KIPKWDLAKF SSQVDRKVGS SMKSVGEVMA IGRTFEESLQ KAIRQVDPRY
VGFEAYVKPE DLDYALSHPT DTRLFAIAYA FFEKHYTVEM VHELTKIDKW FLYKIENIVN
THYALKDAGS VSAINKDLMH QAKRMGFSDV QIASLVKDSE GAVRAHRKSL GVTPFVKRID
TLAAEFPAHT NYLYTTYNAS THDVDFDEHG TMVLGSGVYR IGSSVEFDWC AVTCARKLRD
MGKRTIMINY NPETVSTDFD EADRLYFEEL GWERVMDIYE LEQASGVVVS VGGQLPQNIA
LRLKQSGVNV LGTDPAMIDT AEDRHKFSSI LDKVGVDQPE WTEVSSVGAA KEFANRVGYP
VLIRPSYVLS GAAMNIVYEE STLEHKLSAA ADVSPLHPVV ITKFIDGAQE IDVDAVAHKG
KLLVHAVSEH VEQAGVHSGD ATLVLPPFTL SESVMARVKE IAEKVGAALE ISGPFNMQII
KKDVSDGEPE LKVIECNLRA SRSFPFVSKV LGQNFVDIAT AAIVGQDVPE PVDLMAVKRD
YTAIKVSQFS WTRLGGADPF LGVEMASTGE IASFGKDVYE AYWAAVQSQT GFKNPRPGSG
VLIGGDISKP EMLSIAKKLT ELGFKLYCSS PAVETHLNNP PYLTCKRIFF PTKDKRKLRE
VFDEYEIQCV INLALSRAES ATDEDYVARR NAVDFGLPLL NNAQCAELFV EALARKIPQG
GLRPYTEGKI PSEVKSWAEF VGVRV
//
