ID A0A0N4X5S4_HAEPC Unreviewed; 1455 AA.
AC A0A0N4X5S4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=CAD protein {ECO:0000313|WBParaSite:HPLM_0001971601-mRNA-1};
GN ORFNames=HPLM_LOCUS19708 {ECO:0000313|EMBL:VDO78853.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001971601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001971601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO78853.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO78853.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UZAF01021530; VDO78853.1; -; Genomic_DNA.
DR STRING; 6290.A0A0N4X5S4; -.
DR WBParaSite; HPLM_0001971601-mRNA-1; HPLM_0001971601-mRNA-1; HPLM_0001971601.
DR OMA; ENAAYYY; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
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: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 HAMAP; MF_01209; CPSase_S_chain; 1.
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 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; 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; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 520..712
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1045..1236
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1308..1455
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1455 AA; 160733 MW; 3B4BCD3B54155051 CRC64;
MSWQTMQATL YLCDGSQFSG HLFGATKSVV GEIVFQTGMV GYVESLTDPS YAEQLLVLTY
PIIGNYGVPS QSETDSLGLP MHFESNRVWP AALIVDKICP ENEHSHWKAL ESLSSFLRRA
GVPGLAGIDV RKLTKKIREV GTMKAKIVIE GDEPLKYAFR DINENNLVAA VSRKMPQTFG
SGKNTVLAVD CGMKNNQIRC MVERGMRVKV VPWDYRFENE AFDGLFLSNG PGDPEKCSLL
IDRLTELLGK TTKPVFGICL GHQLLARAAG AQTYKLKYGN RGHNQPCTHE ATGRCFITSQ
NHGFAVDPKT LPAGWQPLFT NENDGTNEGI VHESKPFFSV QFHPEHTGGP ADCEFLFNVF
AEAIDLVKKG MHCSVDELLT SYIRYDSSYQ IRKQRKVLVL GSGGLTIGQA GEFDYSGAQA
LKALKEEGVR TVLINPNVAT VQTSKGFADF TYFLPITKEY VTDVIKKERP TGILVTFGGQ
TALNCAIDLY KDGVFESYDV EVLGTPIETI MNTEDRDRFN KEVISIGEQV APSHAATTLQ
GAIEAAEKIG YPVLVRAAFA LGGLGSGFAE NRSELVAIAQ QALAHSDQVL IDKSLKGWKE
VEYEVVRDAY DNCITVCNME NIDPLGIHTG ESVVVAPSQT LSNKEYNMLR TCAIKVIRHL
GIVGECNIQY ALDPFSHTYY IIEVNARLSR SSALASKATG YPLAYVAAKL ALGQKLPVIR
NSVTGTTTAC FEPSLDYCVV KIPRWDLGKF ARVSQQIGSS MKSVGEVMGI GRSFEEAFQK
ALRMVSDHAD GFSPDAFHRK PTNEDLSNPT DKRMFAIARG MFYGDFNVEK TYALTHIDRW
FLYRMHNIVD IYHKLLKETL MTLSPELLLE AKQAGFSDRQ IAKMVDRRVR LNVTPWVKQI
DTVAGEWPAQ TNYLYVTYNG AENDKNAVIV LGSGVYRIGS SVEFDASCVG CVRELKALGY
QTITVNCNPE TVSTDYDICD RLYFEEISFE TVIDIYHMEK PKGIILAFGG QAPNNIAMSL
SKAQVSIFGT SPNDIDSAED RYKFSRKLEH LQISQPQWKK SDDVEDAKQF CAKVGYPCLI
RPSYVLSGAA MNVAHTEDDL AAFLKQAAVV AKEHPVVVSK FISEAKEIDV DAVAMEGEVL
VMAVCEHVEN AGIHSGDATL VTPPQDLNQV TLNRIQEITV QIASAFNANG PFNMQLIAKD
NELKVIECNL RVSRSFPFVT KTLDFDFVAL ATRAMMAADN PAIASSLKKH GLLRGKARVG
VKVPQFSFSR LTGADVMLGV EMASTGEVAC FGKHRQEAYL KALLSTGFVV PKKNILLSIG
GYHAKSEMLR SVQLLQDMNF DLFGSKGTAD YFQSNNIHVT AVDWPFEEGT SDQKMAAGTR
SVAEFFENKE FHLVINLPIR GSGAYRVSAY RTPGYKTRRM AVDNGIPLIT DIKCAKLFIE
VCCFFFAKAA SYFCY
//
