ID V5DDF4_TRYCR Unreviewed; 917 AA.
AC V5DDF4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamine-dependent carbamoyl-phosphate synthetase {ECO:0000313|EMBL:ESS65466.1};
GN ORFNames=TCDM_06187 {ECO:0000313|EMBL:ESS65466.1};
OS Trypanosoma cruzi Dm28c.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS65466.1, ECO:0000313|Proteomes:UP000017861};
RN [1] {ECO:0000313|EMBL:ESS65466.1, ECO:0000313|Proteomes:UP000017861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dm28c {ECO:0000313|EMBL:ESS65466.1,
RC ECO:0000313|Proteomes:UP000017861};
RX PubMed=24482508;
RA Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL Genome Announc. 2:e01114-13(2014).
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 -!- 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:ESS65466.1}.
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DR EMBL; AYLP01000064; ESS65466.1; -; Genomic_DNA.
DR AlphaFoldDB; V5DDF4; -.
DR EnsemblProtists; ESS65466; ESS65466; TCDM_06187.
DR VEuPathDB; TriTrypDB:TCDM_06187; -.
DR Proteomes; UP000017861; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000017861}.
FT DOMAIN 499..691
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 917 AA; 102332 MW; EC3D4C883ACD4951 CRC64;
MLEEKVKASL VLHGGECFEG YSFGYEESVA GEVVFATGMV GYPEAMTDPS YQGQILVLTS
PMVGNYGIPP IEADHFGLTK YFESMDGKIH VSAVVVSEYC DEPAHWQMWE TLGQWLRRNN
IPGIMMVDTR HIVLKLREMG TALGKVVVND KDVPFVDPNM RHLVAEVSTK TRSTYGHGTL
VILVIDMGVK LNSLRCLLKY DVTLIVVPHD WDITKETYDG LFISNGPGNP QMCTKTIEHV
RWAITQDKPI FGICMGNQIL ALAAGGSTYK MKYGHRGQNQ PSTCRSDGHV FITTQNHGFA
VDFKSVSQDE WEECFYNPND DSNEGLRHRT KPFFSVQFHP EGRCGPQDTE YLFGEFIAHV
KESKVKEASK YKPRKVLVLG AGGIVIAQAG EFDYSGSQCL KALSEEGIET VLVNPNIATV
QTDDEMADQI YFVPITAEAV ERVIEKERPD GIMLAWGGQT ALNCGLEMDR LGILKKYNVQ
VLGTPISTIT VTEDRDLFRN ALLQINEHVA KSLAVTSIEE AVGASKEIGF PLMLRAAYCL
GGQGSGIVYN EEELRHKVGV ALAVSPQVLL EESVAGWKEV EYEVVRDIYD NCITVCNMEN
FDPMGIHTGE SIVVAPSQTL TNDEYHMLRS ASIKIIRHLG IVGECNIQYG LDPSSHRYVV
IEVNARLSRS SALASKATGY PLALVAAKIA LGKGLFEIAN GVTKTTMACF EPSLDYIVVK
VPRWDLSKFN MVSQNIGSMM KSVGEVMAIG RTFEEALQKA LRMVDPSHTG FDVPPRLEAK
KNWDYMQDLK VPTPDRIFAI CRALHEGVSV ETIHEMTRIN LFFLHKLHKL ILLQNHMLQQ
YKGKMNTMPR DYLLKMKANG FSDAQIAKYF LCTVDDVRER RMELKITPKV KQIDTVAGEI
PASQCGFFVY QLQRIPR
//
