ID A5X2K8_9MUSC Unreviewed; 1297 AA.
AC A5X2K8;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:ABC96250.1};
DE Flags: Fragment;
OS Hyperperacera sp. JKM-2006.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Empidoidea;
OC Empididae; Hyperperacera.
OX NCBI_TaxID=369882 {ECO:0000313|EMBL:ABC96250.1};
RN [1] {ECO:0000313|EMBL:ABC96250.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17468014; DOI=10.1016/j.ympev.2007.02.029;
RA Moulton J.K., Wiegmann B.M.;
RT "The phylogenetic relationships of flies in the superfamily Empidoidea
RT (Insecta: Diptera).";
RL Mol. Phylogenet. Evol. 43:701-713(2007).
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DR EMBL; DQ369294; ABC96250.1; -; Genomic_DNA.
DR MEROPS; C26.952; -.
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 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; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 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; 2.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 473..665
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1006..1197
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:ABC96250.1"
FT NON_TER 1297
FT /evidence="ECO:0000313|EMBL:ABC96250.1"
SQ SEQUENCE 1297 AA; 143433 MW; 3F8ABD449DE0899D CRC64;
QILSLTYPMF GNYGVPSEED LDEFGLPRNF EWTDGISVAG LVVGEVCSTP SHWRQTRTLS
KWMENQGIPG ISDIDTRALT KKIRENGSIL GRIAYELPQP GVDLKLSDPN TRNLVAECSV
KKPIVYNPSG SPRICAIDCG LKLNQIRCFI ARGARVELVP WNHNLNASEF DGLFISNGPG
DPVVCKDSVS QIQKILKKSD IPIFGICLGH QLLSTAIGCK TYKMKYGNRG HNLPCVHHGT
GRCFMTSQNH GFAVDAATLP SDWEPLFTNA NDHTNEGIIH KNKPYFSVQF HPEHTAGPED
LEMLFDVFLD AVKEKLTGQK QQKSIKQNLI EKLSYKLNKE SVLPDRPRKV LILGSGGLSI
GQAGEFDYSG SQAIKALKEE KIQTILINPN IATVQTSKGL ADKVYFLPLT PEYVEQVIKA
ERPNGVLLTF GGQTALNCGV ELDRAGVFKK YNVKIMGTPI QSIIETEDRK IFSERVAEIG
EQVAPSEAVY SVAEALEAAE TLGYPVMARA AFSLGGLGSG FANNIEELKI LAKQALAHSN
QLIIDKSLRG WKEVEYEVVR DAFDNCITVC NMENLDPLGI HTGESIVVAP SQTLSNREYN
ILRTTAIKVI RHFGVVGECN IQYALNPESE EYYIIEVNAR LSRSSALASK ATGYPLAYVA
AKLALNVALP DIKNSVTGVT TACFEPSLDY CVVKIPRWDL SKFVRVSKNI GSSMKSVGEV
MAIGRNFEEA FQKALRMVDE TVTGFDPYIK EVKEEELIQA TDKRPYVLAA ALKANYTIEK
LHDLTKIDPW FLNKMKNIID FLNILESQGN NLDHSLLLQA KKLGFSDRAI AEAIKSTDLV
VRSHREQLGV TPFVKQIDTV AGEWPATTNY LYLTYNATTH DIDFPGNFTI VVGSGVYRIG
SSVEFDWCAV GCLRELRKLG RQTIMINYNP ETVSTDYDMC DRLYFEEISF EVVMDIYQFE
NADGIILSMG GQLPNNIAMD LHRQQARVLG TSPESIDSAE NRFKFSRMLD RKGILQPRWK
ELTNLKSAID FCEEVGYPCL VRPSYVLSGA AMNVAYSNQD LETYLNAASL VSKEHPVVIS
KFLQEAKEID VDAVAADGEI LCMAVSEHVE NAGVHSGDAT LVTPPQDLNG QTLEKIKEIV
RDLAALLDVT GPFNMQLIAK NNELKVIECN VRVSRSFPFV SKTLNHDFVA TATRAIIGMA
VEPVEVLHGC GKVGVKVPQF SFSRLAGADV QLGVEMASTG EVACFGDNRH EAYLKAMMST
GFQIPKKAIL LSIGSFKHKV ELLQSIRDLA KMGYKLY
//