ID U7PV35_SPOS1 Unreviewed; 1183 AA.
AC U7PV35;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=HMPREF1624_05396 {ECO:0000313|EMBL:ERS98609.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS98609.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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; KI440846; ERS98609.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PV35; -.
DR STRING; 1391915.U7PV35; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_0_1; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000018087; 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}; Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 232..424
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 769..966
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1034..1183
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1183 AA; 129591 MW; 15CDC30F14001978 CRC64;
MMSAVSMAGR APSRLLRHGR CLPTAVPSTR AAAFSVSTQV QLQQIVHRPQ PKTLKTLNSY
ANTRRTLSQS TKRAATAVDS AVTDSVHDPK AYMQSGVVKP RAEVDVKKVL VIGSGGLAIG
QAGEFDYSGG QALKALKEAG VASVLINPNI ATIQTNHSLA DEVYYLPVTP EYVSYVIERE
KPDGIFLSFG GQTALNLGVE MERRGLFAKY GVRVLGTSVR TLELSEDRDL FARALDEINI
PIAKSIAVST VDEALDAARK IGYPIIVRAA YALGGLGSGF ANNEEELRNM SARSLTLSPQ
ILVEKSLKGW KELEYEVVRD ANNNCITVCN MENFDPLGIH TGDSIVVAPS QTLSDEEYHM
LRSAAIKIVR HLGVVGECNV QYALQPDGLD YRVIEVNARL SRSSALASKA TGYPLAYTAA
KIGLGHTLPE LPNAVTKTTT ANFEPSLDYI VTKIPRWDLS KFQHVKRDIG SAMKSVGEVM
AIGRTFEESF QKAIRQVDPR FVGFQGDKFA DLDFELQNPT DRRWLAVGQA MLHENYSVDR
VHELTKIDKW FLYKLQNIVD TTRELQAVGS LGGLKRELLT KAKKMGFSDR QIASALGSTE
DEVRAVRRQF GIHPWVKKID TLAAEFPANT NYLYTTYNAS THDITFEDKG TVVLGSGVYR
IGSSVEFDWC SVSAARALRA MGKKTVMINN NPETVSTDSD EADRLYFDES SYERVMDIYE
LEQASDVVVS VGGQLPQNIA LRLQETGGAK VLGTDPRNID KAEDRQKFSN ILDNIGVDQP
AWKELTSVDA AAKFAEDVGY PVLVRPSYVL SGAAMTVIHS QEDLKDKLEA ASSVSPDHPV
VISKFIEGAQ EIDVDGVASK GELILHAVSE HIEQAGVHSG DASMILPPVS LDDTTMDRVK
EIAQKVAAAL EITGPFNMQI IKADDPAGGL PALKVIECNL RASRSFPFVS KVLGTNFIDA
ATHALVGEDV PAARDLMKVP RDYVATKVPQ FSWTRLAGAD PFLGVEMSST GEMACFGKDL
VEAYWASVQS AMNFRVPEIG EGLLFGGETS KDWLAKVINF VGPMGYKLYA AEPRVKAFLE
AESKTPIDVQ VIEFPTEDKR QLREVFAKYD IRGVFNLAKA RGKTVQDVDY VMRRNAVDFG
VPLFMEPKTA ILFAQCLSEK LPRAEGTPSE VRRWSDFIGG KPL
//
