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}.
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; 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
//