ID W7AAL9_9APIC Unreviewed; 2184 AA.
AC W7AAL9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Carbamoyl phosphate synthetase {ECO:0000313|EMBL:EUD68770.1};
GN ORFNames=C922_00458 {ECO:0000313|EMBL:EUD68770.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD68770.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD68770.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD68770.1,
RC ECO:0000313|Proteomes:UP000030640};
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 inui San Antonio 1.";
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; KI965461; EUD68770.1; -; Genomic_DNA.
DR RefSeq; XP_008814296.1; XM_008816074.1.
DR EnsemblProtists; EUD68770; EUD68770; C922_00458.
DR GeneID; 20035732; -.
DR VEuPathDB; PlasmoDB:C922_00458; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000030640; 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 763..956
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1768..1959
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 2025..2184
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1286..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 511
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 597
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2184 AA; 247752 MW; 12475C126B8AAB04 CRC64;
MMNTEFWPDY DYKTVGKLIL EDDTEFVGYS VGYEGCKEEE KATPKREATK GSNWNQVLEK
KKYLKEDVLF KNSKIENEDY IVTGEVIFNT AMVGYPEALT DPSYFGQILV LTFPSIGNYG
VEKVLHDNFG LVKNFESNKI QIQGLVICEY TKNSYHYNSC ITLSEWLKLY KVPCIGGIDT
RALTKILRER GSMLGKIVIY KNARNVNKLY KEISLFDPGQ IDTIKYVCNH FIRVIKLGRV
NYYNKGKSKE DSKGTNDAID YSTEEQQNGN SFTNGYNCQS LSSFEKIDFN KNSNQHSLLR
DKMNLLTSSE ENIDHCSGYQ EYSTNGGKKD AFFNLRGACE YDKYLIDLEE NSFFHDGNVD
MYGHYDVEVS LQRSGLSDAG NEEYTTGGRD EGVAPHDEAT FNLKNDYSTY VRKKLNKEEF
LKLVNKRTSD MEKIIVVVDC GIKNSIIKNL MKNGKDLPLT YIIVPYYYDY NSIDYDAVLL
SNGPGDPKKC DSLIETLKKS LQKNKLIFGI CLGNQLLGIS LGCETYKMKY GNRGVNQPVI
QLVDNKCYIT SQNHGYCLKK KSILRRKELA ISYVNANDKS VEGITHKNGR FYSVQFHPEG
NNGPEDTCFL FKNFLIDMFN KKREFREHLG HNIIYIKKKV LLLGSGGLCI GQAGEFDYSG
TQAIKSLKEC GIYVILVNPN IATVQTSKGL ADKVYFLPVN CEFVEKIIKK EKPDFILCTF
GGQTALNCAL MLEQKKILKK NNCLALGTSL ESILITENRS MFAEKLREIN EIIAPYGSAR
NVEQAIEVAN KIGYPILVRT TFSLGGLNSS FINNEEELVK KCKEIFLQTD NEIFIDKSLK
GWKEIEYELL RDNKNNCIAI CNMENIDPLG IHTGDSIVVA PSQTLSNYEY YKFREIALKV
ITHLNIIGEC NIQFGINPKT GEYCIIEVNA RLSRSSALAS KATGYPLAYI SAKIALGYDL
ISLKNSITKK TTACFEPSLD YITTKIPRWD LNKFEFASKT MNSSMKSVGE VMSIGRTFEE
SIQKSLRCID DNYLGFSNTY CIDWDEAKIV DELKNPSPKR IDAIHQAFHL NIPMEKIHEL
TNIEYWFLHK FYNIFNLQNR LKTLSLEELS FYDLKYFKKH GFSDKQIAHY LSFNNPNVSE
AVVMRYRESL GLHPHIKVID TLSAEFPALT NYLYLTYQGV EHDVLPLNMK RKKKLPAQSN
RKKINRAANR GNPHISLQMQ EKKAVKQLQL GGDENGYSET FDNDVDVTVM STKVVGAVGK
QDKIVASNKE GPLFAAEGAQ MNVHASPSNQ MLSKDGKEEK SIGSDETNVF SVKNCTNDVS
FASSLNIVES TMLNNDPQSS TQAGGDSKHI KGSSANNTSK DDGCSKKLQN REILMNHRMD
EISNRSSHST NDQFYLENFN TSDEEMKNKN GDSYYLSKKK KKFSDSKGAG NLYYLVDSVY
NNEYKMSKMK ELINSENTDS NDSLQCEQRG FVVKSGQVGT RFGATSAAED SIPMHVPHYA
GRKINAGIEE SAKGDNLHHH ETERERSKGR SSSRKRESKL NSNGINFDDK NSDCFSELSY
LRNCTKSSDA ENDDIDDDAY CNEGEDVYTC STDNGLFDDY AQSYNTFSSK ESEGSSIYSE
NENIFSEKFN DIGFKIIHDR NEKEKEKKKC LIVLGCGCYR IGSSVEFDWS AIHCVKTIRK
LNHKAILINC NPETVSTDYD ESDRLYFDEI TTEVIKFIYN FEKSHGVIIA FGGQTSNNLV
FSLYKNSVNI LGTSAKSVDC CENRNKFSNL CDSLKIDQPK WNKFTKLSKA IQFANEVKFP
VLVRPSYVLS GAAMRVVNCF EELKNFLMKA AIVSKDNPVV ISKFIENAKE IEIDCVSKNG
KIINYAISEH VENAGVHSGD ATLILPAQNI YVETHRKIKK ISEKISKSLN ISGPFNIQFI
CHQNEIKIIE CNLRASRTFP FISKALNLNF IDLATRILMG YDVKPINISL IDLEYTAVKS
PIFSFNRLHG SDCILGVEMK STGEVACFGL NKYEALLKSL IATGMKLPKK SILISIKNLN
NKLAFEEPFQ LLFLMGFTIY ATEGTYDFYS KFLESFNVTK TSKFHQRLIR VHNKSSENLM
PNITDLIMNH KVEMVINITD TLKTKVSSNG YKIRRLASDF QVPLITNMKL SSLFIDSLYR
KFSRRKEKKP FYTIKSYDEY ISLV
//
