ID D6BUG9_9HYME Unreviewed; 320 AA.
AC D6BUG9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Carbomoylphosphate synthase {ECO:0000313|EMBL:ADD13248.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ADD13248.1};
OS Technomyrmex voeltzkowi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dolichoderinae; Technomyrmex.
OX NCBI_TaxID=628165 {ECO:0000313|EMBL:ADD13248.1};
RN [1] {ECO:0000313|EMBL:ADD13248.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20525640; DOI=10.1093/sysbio/syq012;
RA Ward P.S., Brady S.G., Fisher B.L., Schultz T.R.;
RT "Phylogeny and biogeography of dolichoderine ants: effects of data
RT partitioning and relict taxa on historical inference.";
RL Syst. Biol. 59:342-362(2010).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; FJ939945; ADD13248.1; -; Genomic_DNA.
DR AlphaFoldDB; D6BUG9; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 225..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD13248.1"
FT NON_TER 320
FT /evidence="ECO:0000313|EMBL:ADD13248.1"
SQ SEQUENCE 320 AA; 35004 MW; 602BA7E56BA80790 CRC64;
SQNHGFCVDA SRLPADWEVL FTNKNDNSNE GIVHTSLPYF SVQFHPEHTA GPQDLECLFD
VFLESVQDEI ADGPQISMKD RLTQKLTYEP AVPIAIERPK KVLILGSGGL SIGQAGEFDY
SGSQAIKALK EESIQTVLIN PNIATVQTSK GMADKIYFLP IIAEYVEQVI QSERPNGVLL
TFGGQTALNC GVELEKNGVF AKYNVKILGT PIESIIQTED RKIFADSISE INEKVAPSAA
VYSIQEALEA AEKIGYPVMA RAAYSLGGLG SGFANTKEEL KTLAQKALAH SNQLIIDKSL
KGWKEVEYEV VRDAYDNCIT
//
