ID A0A1A8WDK7_PLAMA Unreviewed; 2218 AA.
AC A0A1A8WDK7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Carbamoyl phosphate synthetase, putative {ECO:0000313|EMBL:SBS90117.1};
DE Flags: Fragment;
GN ORFNames=PMALA_028690 {ECO:0000313|EMBL:SBS90117.1};
OS Plasmodium malariae.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5858 {ECO:0000313|EMBL:SBS90117.1, ECO:0000313|Proteomes:UP000078597};
RN [1] {ECO:0000313|Proteomes:UP000078597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; FLQW01001532; SBS90117.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PmUG01_14024900; -.
DR OMA; YEVEYLY; -.
DR Proteomes; UP000078597; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 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; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
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 PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 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; 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; 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 4: Predicted;
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 775..968
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1802..1993
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 2059..2218
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1541..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 523
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 609
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 611
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SBS90117.1"
SQ SEQUENCE 2218 AA; 253728 MW; 10EFC51E9633D1C7 CRC64;
LILEDNTEFV GYSVGYEGGE GKKVISKNEF IKCDNSNEVI KKKNYVKEDL LFSNSKIENE
EYIVTGEVIF NTAMVGYPEA LTDPSYFGQI LVLTFPSIGN YGVEEVKHNN FGLVENFESN
RIQIQGLVIC EYTKKSYHYN SYITLSEWLK IYKIPCIGGI DTRALTKILR EKGSMLGKIV
IYKNRKNIDK LYKEVSLFDP GQIDTQKYVC NHFIRVFKLS KVSDVHNSKS KEELKAVNDM
NDSLFTDQEN DSNINGSQYN YQRVSSMKKT DYNKDLNNHY VLTNKMNILT SSDENLKDYS
TYYNYNVNSE ENDVFCNSYA LCEYDKYLID VEENSPFHDE NVDEYGYYDV EKSMKKNLIN
DTYSNNDNCG EVFYDSSAMN EKGVKIEEEG MQINNCTYLD SAFNKNSKGV KKFNLNNDYS
TYIKKKMNNE EFLKLVNKRK SDKERIIIIV DCGIKNSIIK NLMKNGKDLP LTYIIVPYYY
DYNYIDYDAV LLSNGPGDPK KCELLIETLR KSLHKNKIVF GICLGNQLLG LSLGCETYKM
KYGNRGVNQP VIQLVDNKCY ITSQNHGYCL KKKNILRRKD ITISYINAND KSVEGIAHKN
GRFYSVQFHP EGNNGPEDTS FLFKNFFLDV FNKKREFREH IGHNIICIKK KVLLLGSGGL
CIGQAGEFDY SGTQAIKSLK ECGIYVILVN PNIATVQTSK GLADKVYFLP VNCEFVEKII
KKEKPDFILC TFGGQTALNC ALMLEQKKVL KKNNCLALGT SLESILITEN RSMFAEKLRE
INEVIAPYGS AKNVEQAIEV ANKIGYPILV RTTFSLGGLN SSFINNEEEL VHKCKEIFLQ
TDNEIFIDKS LRGWKEIEYE LLRDNKNNCI AICNMENIDP LGIHTGDSVV VAPSQTLSNH
EYYKFREIAL KVITHLNIIG ECNIQFGINP KTGEYCIIEV NARLSRSSAL ASKATGYPLA
YISAKIALGY DLISLKNSIT RKTTACFEPS LDYIITKIPR WDLNKFEFAS NTMNSSMKSV
GEVMSIGRTF EESIQKSLRC IDDNYLGFSN TYCIDWEEAK IIDELKNPSP KRIDAIHQAF
HLNIPFEKIQ ELTNIDYWFL YKFYNIFNLQ NKLKTLTLEQ LSFFDLKYYK KYGFSDKQIA
YYLSYNNTKV TESTVMKYRE SLGLHPHIKV IDTLSAEFPA LTNYLYLTYQ GVEHDVLPLN
MKKKKKVMVE GSGKRKESGK NVYNNKNLAV ASEGGIGAYN MKGDKEDKRK LANMFNNDGS
NYINLTKVSN GININEYGVD IDNSNSNSNM FSKHGKEERS IGSDETNMFS VNNSPNNLSF
NNEHNMAQEN VNNENKRETY DSGSSCRNEK NEIKTDKCMK ECLGENNNNY YNHLNGTACN
LRVANASINN KSNDISGKCN YGKDVNIKST NKNDRKVKNK DIGMNTNIEE AISNKSSHST
NDQLYLDNFN TSDEEMANKN IDIYLSKKKK NLTDNKSPGN SYYVVDSVYN NEYKLNKMKE
LINKENADSN YETAQYELDS VTGKYREINK HTLSSNIDDF NKEKGIDAKQ KNEKSRYRSS
SNNNIMRKRS SKKSSICFDN EDKSSDCFSE LSFMRNCSKF SEGESDYMDE DDEDEYVHTS
DSSCYDDYEV EEDEDEAYDS LLSKGSKKSS LHSGHKNIFN EKFNGIEFKI INDRNEKEKE
KKKCFMVLGC GCYRIGSSVE FDWSAIHCVK TIRKLNHKAI LINCNPETVS TDYDESDRLY
FDEITTEVIK FIYNFEKSQG VIIAFGGQTS NNLVFSLYKN NVNILGSSAK SVDCCENRNK
FSHLCDSLKI DQPKWNKFTK LSKAIQFANE VKFPVLVRPS YVLSGAAMRV VNCFEELKNF
LMKAAIVSKD NPVVISKFIE NAKEIEIDCV SKNGKIINYA ISEHVENAGV HSGDATLILP
AQNIYVETHR KIKKISEKIS KSLNISGPFN IQFICHQNEI KIIECNLRAS RTFPFISKAL
NLNFIDLATR ILMGYDVKPF NISLIDLEYT AVKSPIFSFN RLHGSDCILG VEMKSTGEVA
CFGLNKYEAL LKSLVATGMK LPKKSILISI KNLNNKLAFE EPFQLLFLMG FTIYATEGTY
DFYSKFLESF NVSKDSKFHQ RLIRVHNKSS EFLLPNITDL IMNHKVEMVI NITDTLKTKV
SSNGYKIRRL ASDFQVPLIT NMKLSSLFID SLYRKFSRRK EKRSFYTIKS YDEYISLV
//
