ID B4YT24_TRICA Unreviewed; 882 AA.
AC B4YT24;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:ACF35363.1};
DE Flags: Fragment;
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:ACF35363.1};
RN [1] {ECO:0000313|EMBL:ACF35363.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18644735; DOI=10.1016/j.ympev.2008.05.023;
RA Wild A.L., Maddison D.R.;
RT "Evaluating nuclear protein-coding genes for phylogenetic utility in
RT beetles.";
RL Mol. Phylogenet. Evol. 48:877-891(2008).
RN [2] {ECO:0000313|EMBL:ANW44681.1}
RP NUCLEOTIDE SEQUENCE.
RA McKenna D.D., Wild A.L., Kandad K., Bellamy C.L., Beutel R.G.,
RA Caterino M.S., Farnum C.W., Hawks D.C., Ivie M.A., Jameson M.L.,
RA Leschen R.A.B., Marvaldi A.E., McHugh J.V., Newton A.F., Robertson J.A.,
RA Thayer M.K., Whiting M.F., Lawrence J.F., Slipinski A., Maddison D.R.,
RA Farrell B.D.;
RT "The beetle tree of life reveals that Coleoptera survived end-Permian mass
RT extinction to diversify during the Cretaceous terrestrial revolution.";
RL Syst. Entomol. 40:835-880(2015).
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; EU677538; ACF35363.1; -; Genomic_DNA.
DR EMBL; KP813051; ANW44681.1; -; Genomic_DNA.
DR AlphaFoldDB; B4YT24; -.
DR HOGENOM; CLU_000513_2_0_1; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
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 NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 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 200..392
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 734..879
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACF35363.1"
FT NON_TER 882
FT /evidence="ECO:0000313|EMBL:ACF35363.1"
SQ SEQUENCE 882 AA; 97771 MW; 7014C2B1747D7200 CRC64;
LFTNANDKTN EGIIHSKLPF FSVQFHPEHT AGPQDLECLF DVFLDLVKNP NQTAKTLLTQ
KLTYSGTPQL PERPKKVLII GSGGLSIGQA GEFDYSGSQA IKALREENIQ TVLINPNIAT
VQTSKGLADK VYFLPLVPDY VEQVIRVERP GGVLLTFGGQ TGLNCGVELQ KAGIFDKYNI
QILGTPIQAI IDTEDRKIFT ERIAAIGEKV APSMAAHSVE EALEAAEQLG YPVMARAAFS
LGGLGSGFAN SKDELKTLAV QALAHSSQLI IDKSLKGWKE VEYEVVRDAF DNCITVCNME
NVDPLGIHTG ESIVVAPSQT LSNREYNMLR TTAIKVIRHF GVIGECNIQY AVNPNSEEFY
IIEVNARLSR SSALASKATG YPLAYIAAKL ALGVPLPEIN NSVTGVTTAC FEPSLDYCVV
KIPRWDLHKF SRVSTKIGSS MKSVGEVMAI GRKFEEAFQK ALRMVDENVM GFDPYLKDVN
DEELKEPTDK RMFVVAAALK KGYSVDRLYD LTKIDRWFLE KMKKIVDWTT FLETIDQLHL
SHDILLKAKQ IGFSDKQIAT AVKSTELAIR KQREEFGIKP YVKQIDTVAA EWPATTNYLY
LTYNAFEHDL TFEEKHTMVI GSGVYRIGSS VEFDWCAVGC LRELRRLGRK TIMINYNPET
VSTDYDMSDR LYFEEISFEV VMDIYNIEDP VGIILSMGGQ LPNNIAIDLH RQQARILGTS
PDSIDGAENR FKFSRMLDRI GIMQPRWKEL TNLKSAIEFC EEVGYPCLVR PSYVLSGAAM
NVAHSNQDLE TYLNAASDVS KEHPVVISKF ILESKEIDVD AVACDGVILC MAVSEHVENA
GVHSGDATLV TPPQDINDET LGKITQICKA IAASLEVTGP FN
//
