ID G0S6C8_CHATD Unreviewed; 454 AA.
AC G0S6C8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carbamoyl phosphate synthase arginine-specific small chain {ECO:0000256|ARBA:ARBA00044168};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE AltName: Full=Arginine-specific carbamoyl phosphate synthetase, glutamine chain {ECO:0000256|ARBA:ARBA00044340};
DE AltName: Full=Glutamine-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044334};
GN ORFNames=CTHT_0034460 {ECO:0000313|EMBL:EGS21583.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS21583.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00043737};
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 CarA family.
CC {ECO:0000256|ARBA:ARBA00007800}.
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DR EMBL; GL988041; EGS21583.1; -; Genomic_DNA.
DR RefSeq; XP_006693879.1; XM_006693816.1.
DR AlphaFoldDB; G0S6C8; -.
DR STRING; 759272.G0S6C8; -.
DR GeneID; 18257484; -.
DR KEGG; cthr:CTHT_0034460; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_035901_1_0_1; -.
DR OMA; CFSVQYH; -.
DR OrthoDB; 2783936at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 54..193
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT ACT_SITE 310
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 454 AA; 49766 MW; 2402392F10D5055D CRC64;
MFSRLAARLP FKAMGHAARL PSQTRFASKL TVSGSKGRTM PATNTRTTAP ASGVNATFTI
RDGPVFHGKA FGANINISGE AVFTTSLVGY PESMTDPSYR GQILVFTQPL IGNYGVPSNE
RDEYNLLKYF ESPHIQCAGI VVADVAEKYS HWTAVESLAE WCAREGIPAI TGVDTRAIVT
YLREQGSSLA RITIGDEYDA DEDEGYVDPG QINLVKRVST KAPFVVNNPN ARYHIALIDC
GVKENILRSL VTRGASITVF PYDYPIHKVA DHFDGVFISN GPGDPTHCQE TVYNLARLME
TSSAPIMGIC LGHQLLALAV GARTIKLKYG NRAHNIPALD LTTGQCHITS QNHGYAVDAS
TLPSEFKEYF VNLNDGSNEG MIHKTRPIFS TQFHPEAKGG PMDSAYLFDK YLENVEMYKA
SAKVYRDNRP SQLMIDILSK ERVGVEPTPL ANYA
//
