ID A0A024W4D6_PLAFA Unreviewed; 2378 AA.
AC A0A024W4D6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:ETW35036.1};
GN ORFNames=PFTANZ_04289 {ECO:0000313|EMBL:ETW35036.1};
OS Plasmodium falciparum Tanzania (2000708).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036725 {ECO:0000313|EMBL:ETW35036.1, ECO:0000313|Proteomes:UP000030708};
RN [1] {ECO:0000313|EMBL:ETW35036.1, ECO:0000313|Proteomes:UP000030708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tanzania (2000708) {ECO:0000313|Proteomes:UP000030708};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum Tanzania (2000708).";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW35036.1, ECO:0000313|Proteomes:UP000030708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tanzania (2000708) {ECO:0000313|Proteomes:UP000030708};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum Tanzania (2000708).";
RL Submitted (FEB-2013) 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; KI926497; ETW35036.1; -; Genomic_DNA.
DR EnsemblProtists; ETW35036; ETW35036; PFTANZ_04289.
DR eggNOG; KOG0370; Eukaryota.
DR Proteomes; UP000030708; 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 Reference proteome {ECO:0000313|Proteomes:UP000030708};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 805..998
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1962..2153
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 2219..2378
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 386..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1749..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1790
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 553
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 641
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2378 AA; 273873 MW; A01667FE2D0ABEB6 CRC64;
MTSEFWPDLD FKTVGRLILE DGNEFVGYSV GYEGCKGNNS ISCHKEYRNI INNDNSKNSN
NSFCNNEENN LKDDLLYKNS RLENEDFIVT GEVIFNTAMV GYPEALTDPS YFGQILVLTF
PSIGNYGIEK VKHDETFGLV QNFESNKIQV QGLVICEYSK QSYHYNSYIT LSEWLKIYKI
PCIGGIDTRA LTKLLREKGS MLGKIVIYKN RQHINKLYKE INLFDPGNID TLKYVCNHFI
RVIKLNNITY NYKNKEEFNY TNEMITNDSS MEDHDYEING SISNFNNCPS ISSFDKSESK
NVINHTLLRD KMNLITSSEE YLKDLHNCNF SNSSDKNDSF FKLYGICEYD KYLIDLEENA
SFHYNNVDEY GYYDVNKNTN ILSNNKIEQN NNNENNKNNK NNKNNNNNEV DYIKKDKDNN
VNSKVFYSQY NNNAQNNEHT EFNLNNDYST YIRKKMKNEE FLNLVNKRKV DHKEKIIVIV
DCGIKNSIIK NLIRHGMDLP LTYIIVPYYY NFNHIDYDAV LLSNGPGDPK KCDFLIKNLK
DSLTKNKIIF GICLGNQLLG ISLGCDTYKM KYGNRGVNQP VIQLVDNICY ITSQNHGYCL
KKKSILKRKE LAISYINAND KSIEGISHKN GRFYSVQFHP EGNNGPEDTS FLFKNFLLDI
FNKKKQYREY LGYNIIYIKK KVLLLGSGGL CIGQAGEFDY SGTQAIKSLK ECGIYVILVN
PNIATVQTSK GLADKVYFLP VNCEFVEKII KKEKPDFILC TFGGQTALNC ALMLDQKKVL
KKNNCQCLGT SLESIRITEN RTLFAEKLKE INERIAPYGS AKNVNQAIDI ANKIGYPILV
RTTFSLGGLN SSFINNEEEL IEKCNKIFLQ TDNEIFIDKS LQGWKEIEYE LLRDNKNNCI
AICNMENIDP LGIHTGDSIV VAPSQTLSNY EYYKFREIAL KVITHLNIIG ECNIQFGINP
QTGEYCIIEV NARLSRSSAL ASKATGYPLA YISAKIALGY DLISLKNSIT KKTTACFEPS
LDYITTKIPR WDLNKFEFAS NTMNSSMKSV GEVMSIGRTF EESIQKSLRC IDDNYLGFSN
TYCIDWDEKK IIEELKNPSP KRIDAIHQAF HLNMPMDKIH ELTHIDYWFL HKFYNIYNLQ
NKLKTLKLEQ LSFNDLKYFK KHGFSDKQIA HYLSFNTSDN NNNNNNISSC RVTENDVMKY
REKLGLFPHI KVIDTLSAEF PALTNYLYLT YQGQEHDVLP LNMKRKKICT LNNKRNANKK
KVHVKNHLYN ELVDDKDTQL HKENNNNNNM NSGNVENKCK LNKESYGYNN SSNCINTNNI
NIENNICHDI SINKNIKVTI NNSNNSISNN ENVETNLNCV SERAGSHHIY GKEEKSIGSD
DTNILSAQNS NNNFSCNNEN MNKANVDVNV LENDTKKRED INTTTVFMEG QNSVINNKNK
ENSSLLKGDE EDIVMVNLKK ENNYNSVINN VDCRKKDMDG KNINDECKTY KKNKYKDMGL
NNNIVDELSN GTSHSTNDHL YLDNFNTSDE EIGNNKNMDM YLSKQKSISN KNPGNSYYVV
DSVYNNEYKI NKMKELIDNE NLNDEYNNNV NMNCSNYNNA SAFVNGKDRN DNLENDCIEK
NMDHTYKHYN RLNNRRSTNE RMMLMVNNEK ESNHEKGHRR NGLNKKNKEK NMEKNKGKNK
DKKNYHYVNH KRNNEYNSNN IESKFNNYVD DINKKEYYED ENDIYYFTHS SQGNNDDLSN
DNYLSSEELN TDEYDDDYYY DEDEEDDYDD DNDDDDDDGE DEEDNDYYND DGYDSYNSLS
SSRISDVSSV IYSGNENIFN EKYNDIGFKI IDNRNEKEKE KKKCFIVLGC GCYRIGSSVE
FDWSAIHCVK TIRKLNHKAI LINCNPETVS TDYDESDRLY FDEITTEVIK FIYNFENSNG
VIIAFGGQTS NNLVFSLYKN NVNILGSSAQ SVDCCENRNK FSHLCDSLKI DQPKWNKFTK
LSKAIQFANE VKFPVLVRPS YVLSGAAMRV VNCFEELKNF LMKAAIVSKD NPVVISKFIE
NAKEIEIDCV SKNGKIINYA ISEHVENAGV HSGDATLILP AQNIYVETHR KIKKISEKIS
KSLNISGPFN IQFICHQNEI KIIECNLRAS RTFPFISKAL NLNFIDLATR ILMGYDVKPI
NISLIDLEYT AVKAPIFSFN RLHGSDCILG VEMKSTGEVA CFGLNKYEAL LKSLIATGMK
LPKKSILISI KNLNNKLAFE EPFQLLFLMG FTIYATEGTY DFYSKFLESF NVNKGSKFHQ
RLIKVHNKNA ENISPNTTDL IMNHKVEMVI NITDTLKTKV SSNGYKIRRL ASDFQVPLIT
NMKLCSLFID SLYRKFSRQK ERKSFYTIKS YDEYISLV
//
