ID A0A0N1I157_LEPSE Unreviewed; 1838 AA.
AC A0A0N1I157;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative carbamoyl-phosphate synthase {ECO:0000313|EMBL:KPI82958.1};
GN ORFNames=ABL78_8027 {ECO:0000313|EMBL:KPI82958.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI82958.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI82958.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI82958.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI82958.1}.
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DR EMBL; LJSK01000475; KPI82958.1; -; Genomic_DNA.
DR EnsemblProtists; KPI82958; KPI82958; ABL78_8027.
DR VEuPathDB; TriTrypDB:Lsey_0475_0020; -.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000038009; Unassembled WGS sequence.
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 Pfam; PF02142; MGS; 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 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.
DR PROSITE; PS51855; MGS; 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 1041..1232
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1299..1484
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
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 1838 AA; 205284 MW; 2D63A1582DA9D237 CRC64;
MEHCVKAELV LHGGECFEGY SFGYESSVAG EVVFTTGMVG YPESLTDPSY QGQILVMTAP
MVGNYGVPAL EEDCFGVTKH FESVNGRIHV SAVVVQEYCD QPDHWQMYES LGQWLRKHKV
PGMMMVDTRS IVLKLRDMGT ALGKVLIGGH DVPFADPNTR NLVAEVSTKT RITYGHGTLR
ILVIDMGVKL NTLRCLLKHD VTVVVVPHDW DITTEVYDGL FISNGPGNPQ MCTSTIRSVR
WALQQSKPIF GICMGNQVLC LAAGGTTFKM KYGHRGQNQP CKCNLDGRVV ITTQNHGFAV
DFKSLPADEW VEYFTNPNDN SNEGLWHKTK PFCSVQFHPE GRCGPQDTEF LFGEYVERVK
EAKVKGLAKF KPRKVLVLGA GGIVIAQAGE FDYSGSQCLK SLRDEGVETV LINPNIATVQ
TDDEMADHIY FVPLTVEAVE RVIEKERPDG IMLGWGGQTA LNCGLKLDEL GILKKYHVQV
LGTPVSVIAV TEDRELFRDA LLQIGEQVAK SAAVTSVEEA IATSHTIGFP MMVRAAYCLG
GQGSGIVENQ EELRQKVEVA LATSPQVLLE ESVAGWKEIE YEVVRDIYDN CITVCNMENF
DPMGIHTGES IVVAPSQTLS NDEFHMLRSA SIKIIRHLGI VGECNIQYGL HPFSHRYVVI
EVNARLSRSS ALASKATGYP LAHVATKIAL GKGLFEIMNG VTKTTMGCFE PSMDYIAVKM
PRWDLSKFNM VSEKIGSMMK GVGEVMSIGR TFEEALQKAI RMVDPSYVGF SVPAQFRGPD
FDYMEHIRHP TPYRMFALCR AMQEGHSVEE LYTLTKITRF FLYKLEKILQ VYSAAARLYR
GKLSETPREF LLNLKAHGFS DRQLADCFDC TPGDVRARRV EMNVMPLIKQ IDTVAGEYPA
AHCCYLYTTY NAQRDDVMFT ERMYAVLGCG VYRIGNSVEF DYGGVLVARE LRRLGNKVIL
INYNPETVST DYDECDRLYF DEVSEETVMD ILTKERVRGV VISLGGQVVQ NMALNLKKAG
LPILGTDPAN IDMAEDRNKF SKMCDDLGVP QPAWISATSV EQVHQFCELV GYPALVRPSY
VLSGSAMAVI SNKEDVTRYL KEASLVSGEH PVVVSKYYED AMEYDVDIVA HHGRVLCYAI
CEHVENAGVH SGDATMLLPP QNTDKETMKR IYDSASCIAE RLDVVGPMNV QFLLADGHLR
VIEANVRSSR SVPFVSKTLG ISFPAVMVSA FLARKDQYLV PIKRAKMTHI GCKASMFSFN
RLAGADPILG VEMASTGEIG VFGRNKHEVF LKAMLCQNFT VPKKGIFFSS DVDSMTGALC
PYVKLLVQKQ LSIYCSTQTA AVLSEYGIEC QVLKQRFEMP QLKEGELSQY EAEVAKREKF
DMVIQIRDKK RDFVLRRCTR ETASPDYWVR RLAVDYNIPL LTEPNIVKLF CECMDLAPSA
MEIEPFRHYV PKIYHRIENN NCAMLRRHKV GLMITNNNDS KVLALRLSQE GLNITCFHAY
LGGSDIDHFE EAFSNLKVPL EVVDLRSEIA SVAFDLIMCQ SADENRNWHL SKLSWHIFGS
FLLLAMRDKH MTVVAQTSKQ SKKEAGFEKY VQSNCPEMGV YNAWRDARLM EDFQSSTDQI
SFLRKHGIKA TVRNNGQVHS SVCGNTYYCD DVRSLPPCTL VKPIRECSPT PEFVSLTFSG
ARCVKINGVN VTPLLALQMA NEIAGRNGCG VTRTREGAMF EAPGMCLLSV GLQFLYDVSF
DRSAADLFRM YSRHVSANIA IGQLAEKHTQ SAIEAVRFLT SDVNGVVELE LHHGEIIFLK
LSHVQNPVDR HMVHQLVTED ELEEVFQPGN GSFSDVQW
//
