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Database: UniProt
Entry: A9QH06_9MUSC
LinkDB: A9QH06_9MUSC
Original site: A9QH06_9MUSC 
ID   A9QH06_9MUSC            Unreviewed;       311 AA.
AC   A9QH06;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=CADr {ECO:0000313|EMBL:ABX75395.1};
OS   Melaloncha acoma.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC   Phoridae; Metopinini; Melaloncha.
OX   NCBI_TaxID=461990 {ECO:0000313|EMBL:ABX75395.1};
RN   [1] {ECO:0000313|EMBL:ABX75395.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=7 {ECO:0000313|EMBL:ABX75395.1};
RX   AGRICOLA=IND44083153; DOI=10.1603/0013-8746(2008)101[713:UODSFI]2.0.CO;2;
RA   Smith P.T., Brown B.V.;
RT   "Utility of DNA Sequences for Inferring Phylogenetic Relationships and
RT   Associating Morphologically Dissimilar Males and Females of the Bee-Killing
RT   Flies, Genus Melaloncha (Diptera: Phoridae).";
RL   Ann. Entomol. Soc. Am. 101:713-721(2008).
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; EU068546; ABX75395.1; -; Genomic_DNA.
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          245..290
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABX75395.1"
FT   NON_TER         311
FT                   /evidence="ECO:0000313|EMBL:ABX75395.1"
SQ   SEQUENCE   311 AA;  33751 MW;  04B07CDBBF3640C8 CRC64;
     FMTSQNHGFA VDANTLPGDW EPLFTNANDF SNEGIIHKTK PYFSVQFHPE HAAGPEDLEL
     LFDLFLEAVK EHXXXXXXXX XXXXXXXXXX XSGPLCVRER LIEKLAYAPK AGSIPEIQPK
     KVLILGSGGL SIGQAGEFDY SGSQAIKALR EEKIQTILIN PNIATVQTSK GLADKVYFLP
     LTKEYVEQVI KAERPNGALL TFGGQTALNC GVELEKAGVF SKYNVKILGT PITSIIETED
     RKIFADRVAE IGEKVAPSEA VYSVQETLEA AEKLGYPVMV RAAFSLGGLG SGFADNVEEL
     KVLATQALAH S
//
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