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Database: UniProt
Entry: D4NZK2_9MUSC
LinkDB: D4NZK2_9MUSC
Original site: D4NZK2_9MUSC 
ID   D4NZK2_9MUSC            Unreviewed;       293 AA.
AC   D4NZK2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE   Flags: Fragment;
GN   Name=CAD {ECO:0000313|EMBL:ADD64224.1};
OS   Melaloncha gibberosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC   Phoridae; Metopinini; Melaloncha.
OX   NCBI_TaxID=710890 {ECO:0000313|EMBL:ADD64224.1};
RN   [1] {ECO:0000313|EMBL:ADD64224.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Brown B.V., Smith P.T.;
RT   "The bee-killing flies, genus Melaloncha Brues (Diptera: Phoridae): a
RT   combined molecular and morphological phylogeny.";
RL   Syst. Entomol. 35:649-657(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR   EMBL; GU550280; ADD64224.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4NZK2; -.
DR   MEROPS; C26.956; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; IPR017926; GATASE.
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; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          227..272
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADD64224.1"
FT   NON_TER         293
FT                   /evidence="ECO:0000313|EMBL:ADD64224.1"
SQ   SEQUENCE   293 AA;  31923 MW;  56E9F66A312D519E CRC64;
     FMTSQNHGFA VDANTLPSDW EPLFTNANDY SNEGIIHKNK PYFSVQFHPE HAAGPEDLEL
     LFDLFLEAVK EHNSGPVCVR ERLIEKLAYF PKTGSFPETQ PKKVLILGSG GLSIGQAGEF
     DYSGSQAIKA LRENKIQTIL INPNIATVQT SKGLADKVYF LPLTKEYVEQ VIKAERPDGA
     LLTFGGQTAL NCGVELEKAG VFSKYNVKIL GTPITSIIET EDRKIFADRV AEIGEKVAPS
     EAVYSVQETL EAAEKLGYPV MVRAAFSLGG LGSGFADNVE ELKILATQAL AHS
//
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