ID G0UM16_TRYCI Unreviewed; 1834 AA.
AC G0UM16;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative glutamine hydrolysing (Not ammonia-dependent) carbomoyl phosphate synthase {ECO:0000313|EMBL:CCC90678.1};
GN ORFNames=TCIL3000_5_4250 {ECO:0000313|EMBL:CCC90678.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC90678.1};
RN [1] {ECO:0000313|EMBL:CCC90678.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC90678.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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};
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DR EMBL; HE575318; CCC90678.1; -; Genomic_DNA.
DR VEuPathDB; TriTrypDB:TcIL3000_5_4250; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00068; UER00113.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-EC.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
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; 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 Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR048268; Arginosuc_syn_C.
DR InterPro; IPR024074; AS_cat/multimer_dom_body.
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; 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; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF20979; Arginosuc_syn_C; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
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 SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 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; 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; 1.
DR PROSITE; PS00867; CPSASE_2; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 498..690
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1043..1235
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1834 AA; 204406 MW; D2B39E2502C8DDCD CRC64;
MRQGVTAELV LHGGERFSGV SFGYEESVAG EVVFTTGMVG YPESLTDPSF HGQILVLTSP
MVGNYGIPAL ETDHFGVTKY FESMNGKIHV SALVVCECCE EPSHWQMHET LGSWLKRNKI
PGIMMVDTRS IVLKLRDMGT ALGKVIVGGA DVPFIDPNTR NLVAEVSTTE RRSYGHGTLN
ILVIDMGVKL NSLRCLLRYD VTLTVVPHDW DITKETYDGL FISNGPGNPQ LCTKTIENVR
WALTQEKPIF GVCMGNHMLA LAAGGSTYKM KFGHRGQNQP STANEDGRVV ITTQNHGFAV
DFKSMPQAEW EEYFFNPNDQ CNEGLRHRTK PFSSVQFHPE GCGGPQDTEY LFEEFICQVK
KSKTKVAALF KPHKVLVLGA GGIVIAQAGE FDYSGSQCLK ALREEGVETV LVNPNIATVQ
TDDEMADRVY FVPVTPEAVE RVIDKERPDG IMLGWGGQTA LNCGLQLDKL GILKKYNVRV
LGTATSTIAV TEDRELFRNA LLQINEPVAK SAAVNSVQEA LEVAADIGFP MMVRAAFCLG
GQGSGIVNDE EELRHKVEMA LAAAPQVLLE ESVAGWKEIE YEIVRDIHDN CITVCNMENL
DPMGIHTGES IVVAPSQTLT NDEYHMLRTA AIKIIRHLGV VGECNIQYGL EPRSRRYVVI
EVNARLSRSS ALASKATGYP LAHVAAKIAL GKGLFEIKNG VTKTTMACFE PSLDYIIVKA
PRWDVAKFNM VSHDIGSMMK SVGEVMAIGR TFEEAMQKAL RMVDPSHTGF DVPDRLTKMG
DKWDYMTNLR VPTPDRIFAV CRALKEGVSI QEVHDITRID KFFLFKLQHL VEMQRDLETL
YRGKLSSITH EHLLSAKSNG FSDVQIARYL ECTPDDVRKR REELKISPKV KQIDTVAGEY
PAAQCCYLYT SYNAQRDDVE FKDRMYAVLG CGVYRIGSSV EFDYCGVLVA RELRRLGNKV
ILINYNPETV STDYDECDRL YFEEVSEESV LDILLKENVL GVIISLGGQI VQNMALRLKE
HGLPILGTDP VNVDKAEDRH KFSKMCDQLG VPQPEWILSS SVEQVHEFCQ RVGFPTLVRP
SYVLSGSAMA VISSTADIDR YLSKASLVSG VHPVVVSKYY EGAMEYDVDI VAHHGRVLCY
AICEHLENAG VHSGDATMFL PPQYTKKEIM KRIYDAATRI AEELDVVGPM NVQFLLTKDE
QLRVIEANIR SSRSVPFVSK TLGISFPAVM VSALLSRRDS DLVPIRRAKM AHIGCKAPMF
SFNRLAGADP ILGVEMASTG EIGVFGRDKR EVFLKAMLCQ NFKYPTKGVF ISCDVDAACE
ELIPYILRMS QKFPLFSSRQ TGVILAKHGI AHEVLTQRHE DTSNPTYEAK LASKAFDLVI
QLRDKRNDFV LRTCTQDTAP PDYWVRRLAV DYNIALLTEP NVVKMFCDSL DVPIESIEIE
PFRHYVPRVY HKIESNNCTM LRHHKVGLCI SPTTDSKVLA MRMNEERIAL TCFHAFLGGL
VTSSEAVAEE FRLVGVPVEV VDLRNEMAEL GFDMVMALIA DEDNNWHLPM LGEHVIGVHL
LQTMRERGVT VVAQCSSHGK KGMNFERYAR MLQPKMGVYS PWRDPRMLSD FPSEEEKVKF
LEQHGVKVQP SLLETHSSVC GITYQLNDTR SAPAPRMVVS PRGCPKAPEF CSITFRAARC
IRINGTDVTP LQALQMANEI GGRNGVGLVR THDGAMYEAP GMALLSKALH FIYDVCFDRS
TTDAFRMYSQ HILSMLAARG LIERHTQSSL EAIRYLTADV GGVVDVELNQ GEVIFLKVSH
VTRPVKLRLA KIMTAEEMEE VFQPGDGTFS DVQW
//
