ID K7Z5F0_9DIPT Unreviewed; 571 AA.
AC K7Z5F0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative CAD trifunctional protein {ECO:0000313|EMBL:AFY05180.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:AFY05180.1};
OS Bittacomorpha sp. BMW-2012.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Ptychopteridae;
OC Bittacomorphinae; Bittacomorpha.
OX NCBI_TaxID=1262259 {ECO:0000313|EMBL:AFY05180.1};
RN [1] {ECO:0000313|EMBL:AFY05180.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21402926; DOI=10.1073/pnas.1012675108;
RA Wiegmann B.M., Trautwein M.D., Winkler I.S., Barr N.B., Kim J.W.,
RA Lambkin C., Bertone M.A., Cassel B.K., Bayless K.M., Heimberg A.M.,
RA Wheeler B.M., Peterson K.J., Pape T., Sinclair B.J., Skevington J.H.,
RA Blagoderov V., Caravas J., Kutty S.N., Schmidt-Ott U., Kampmeier G.E.,
RA Thompson F.C., Grimaldi D.A., Beckenbach A.T., Courtney G.W., Friedrich M.,
RA Meier R., Yeates D.K.;
RT "Episodic radiations in the fly tree of life.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5690-5695(2011).
RN [2] {ECO:0000313|EMBL:AFY05180.1}
RP NUCLEOTIDE SEQUENCE.
RA Caravas J., Friedrich M.;
RT "Shaking the Diptera tree of life: performance analysis of nuclear and
RT mitochondrial sequence data partitions.";
RL Syst. Entomol. 38:93-103(2013).
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; KC177126; AFY05180.1; -; mRNA.
DR AlphaFoldDB; K7Z5F0; -.
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; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 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; IPR013815; ATP_grasp_subdomain_1.
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; 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; 2.
DR Pfam; PF02787; CPSase_L_D3; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 16..79
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 420..571
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFY05180.1"
FT NON_TER 571
FT /evidence="ECO:0000313|EMBL:AFY05180.1"
SQ SEQUENCE 571 AA; 63899 MW; DA5D2C1F157B633C CRC64;
VVAPSQTLSN REYNMLRTTA IKVIRHLGVV GECNIQYALN PYSEEYFIIE VNARLSRSSA
LASKATGYPL AYVAAKLALC IPLPDILNSV TGKTTACFEP SLDYCVVKMP RWDLAKFVRV
SKNIGSSMKS VGEVMAVGRT FEEAFQKALR MVDENVNGFD PYLKSVNENE LTQPTDKRMF
VLAAALRAGY TVDKLYELTK IDRWFLQKMK NIIDHLVFME QNKNHLSREV LLKSKKMGYS
DKQIAAAIRS TELAVRKERR ETNVLPYVKQ IDTVAGEWPA TTNYLYLTYN ASEHDIDFPG
GHTIVVGSGV YRIGSSVEFD WCAVGCLREL RQLGRKTVMI NYNPETVSTD YDMCDRLYFE
EISFEVVMDI YNQENPEGII LSMGGQLPNN IAMDLHRQQA HILGTSPESV DGAENRFKFS
RMLDRRGILQ PRWKELTNLQ AAIEFCEEVG YPCLVRPSYV LSGAAMNVAH SNQDLETYLN
AASDVSKEHP VVISKFLTEA KEIDVDAVAA DGEILCLAVS EHIENAGVHS GDATLVTPPQ
DINAETLDKI KGIAREIAAL LDVTGPFNMH F
//
