ID D0USX3_HEXLM Unreviewed; 200 AA.
AC D0USX3;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Pyrimidine biosynthesis {ECO:0000313|EMBL:ACY45839.1};
DE Flags: Fragment;
OS Hexagenia limbata (Mayfly) (Ephemera limbata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Palaeoptera; Ephemeroptera; Scapphodonta; Ephemeridae; Hexagenia.
OX NCBI_TaxID=244977 {ECO:0000313|EMBL:ACY45839.1};
RN [1] {ECO:0000313|EMBL:ACY45839.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20147900; DOI=10.1038/nature08742;
RA Regier J.C., Shultz J.W., Zwick A., Hussey A., Ball B., Wetzer R.,
RA Martin J.W., Cunningham C.W.;
RT "Arthropod relationships revealed by phylogenomic analysis of nuclear
RT protein-coding sequences.";
RL Nature 463:1079-1083(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};
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DR EMBL; GQ888266; ACY45839.1; -; mRNA.
DR AlphaFoldDB; D0USX3; -.
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; 3.30.470.20; 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; 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 PRINTS; PR00098; CPSASE.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 2: Evidence at transcript level;
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 105..193
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACY45839.1"
FT NON_TER 200
FT /evidence="ECO:0000313|EMBL:ACY45839.1"
SQ SEQUENCE 200 AA; 21213 MW; 646C1FF2A4FF474A CRC64;
SGSQALKALR EEGVLSVLIN PNIATVQTSP GFADKIYFLP ITPEYVEEVI KNERPDGVLL
TFGGQTALNC GVALDAAGVF DKYGVTILGT QIDAINISED RQLFSDKMAS LGEKVAPNIA
VYSVAEALEA AEKLGYPVLA RAAFALGGLG SGFANSPAQL TALAQQALAH SKQLIIDKSL
KGWKEVEYEV VRDVNDNCIT
//