ID Q6WLA3_9MUSC Unreviewed; 1299 AA.
AC Q6WLA3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=CAD {ECO:0000313|EMBL:AAQ67184.1};
DE Flags: Fragment;
GN Name=r {ECO:0000313|EMBL:AAQ67184.1};
OS Meghyperus sudeticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Empidoidea;
OC Atelestidae; Meghyperus.
OX NCBI_TaxID=192519 {ECO:0000313|EMBL:AAQ67184.1};
RN [1] {ECO:0000313|EMBL:AAQ67184.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15019631; DOI=10.1016/S1055-7903(03)00284-7;
RA Moulton J.K., Wiegmann B.M.;
RT "Evolution and phylogenetic utility of CAD (rudimentary) among Mesozoic-
RT aged Eremoneuran Diptera (Insecta).";
RL Mol. Phylogenet. Evol. 31:363-378(2004).
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; AY280688; AAQ67184.1; -; Genomic_DNA.
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 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; 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; 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 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 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; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 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 472..664
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1005..1196
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAQ67184.1"
FT NON_TER 1299
FT /evidence="ECO:0000313|EMBL:AAQ67184.1"
SQ SEQUENCE 1299 AA; 143489 MW; 0623C9C480856AE6 CRC64;
QILILTYPLI GNYGVPSEED LDEYGIPKHF EWTEGISVAG LVVGEICEXP XXWXQTKTLS
KWMEEQGVPG ISDIDTRALT KRIRENGSIL GRITYNFPSP GSDLKLSDPN IRNLVSECSV
KKITVFNQKG SPRICAIDCG LKLNQIRCFL ARGARVDLVP WNHELNAEEF DGLFISNGPG
DPVVCNETVK QIQRILKTSD KPIFGICLGH QLLSTAIGCK TFKMKYGNRG HNLPCIHHGT
GRCFMTSQNH GFAVDVKTLP TDWEPLFTNA NDNTNEGIIH KDKPYFSVQF HPEHSAGPED
LELLFDIFLD AVRVNMTGNA GLSVKQNLME KLNYIPPPNS VLEQKPRKVL ILGSGGLSIG
QAGEFDYSGS QAIKALKEEK IQTILINPNI ATVQTSKGLA DKVYFLPLTP DYVEQVIKAE
RPNGVLLTFG GQTALNCGVE LDKAGVFKKY NVKILGTPIQ SIIETEDRKV FAEKVGEIGE
KVAPSEAVYS VGEALEAAER LGYPVMARAA FSLGGLGSGF ANNTTELTVL AQQALAYSNQ
LIIDKSLKGW KEVEYEVVRD AFDNCITVCN MENLDPLGIH TGESIVVAPS QTLSNREYNM
LRTTAIKVIR HFGVIGECNI QYALNPKSEE YYIVEVNARL SRSSALASKA TGYPLAYVAA
KLALSVPLPD IKNSVTGVTT ACFEPSLDYC VVKIPRWDLA KFVRVSKNIG SSMKSVGEVM
SIGRNFEEAF QKALRMVDET VNGFDPYIKA VIEIELVEPT DKRTFVLAAA LKANYTVEKL
NELTNIDPWF LNKMKNIIEH LNFLESHGNN LTQEMLLQAK KMGFSDRQIS AAIKSTDLVV
RRQREELGVT PFVKQIDTVA GEWPATTNYL YLTYNATSHD IKFPGSFIIV LGSGVYRIGS
SVEFDWCAVG CIKELRNLGK STIMINCNPE TVSTDYDMCD RLYFEEISFE VVMDIYQIEN
ADGIILSMGG QLPNNIAMDL HRQQARVLGT SPECIDTAEN RFKFSRMLDR KGILQPRWKE
LTNLKSAIEF CEHVGYPCLV RPSYVLSGAA MNVAYSNQDL ETYLNAASLV CKEHPVVISK
FLQEAKEIDV DAVAADGEIL CMAVSEHVEN AGVHSGDATL VTPPQDINAE TLERIKEITR
DLAALLDVTG PFNMQLIAKN NQLKVIECNV RVSRSFPFVS KTLNHDFVAT ATRAIIGMPV
EPVDVLHGCG KVGVKVPQFS FSRLAGADVQ LGVEMASTGE VACFGDNRYE AYLKAMMSTG
FQIPKKAILL SIGSFKHKVE LLPSIRDLAK MGYKLYASM
//
