UniProt: U4TYH6

Database: UniProt
Entry: U4TYH6_DENPD

LinkDB:  U4TYH6_DENPD 
Original site:  U4TYH6_DENPD

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Ontology (10)   
   GO (10)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (37)   
   InterPro (21)   
   Pfam (7)   
   PROSITE (6)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (49)   

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ID   U4TYH6_DENPD            Unreviewed;      1701 AA.
AC   U4TYH6;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERL83341.1};
GN   ORFNames=D910_00241 {ECO:0000313|EMBL:ERL83341.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL83341.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL83341.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(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};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC   -!- SIMILARITY: Belongs to the CarB family.
CC       {ECO:0000256|ARBA:ARBA00009799}.
CC   -!- SIMILARITY: Belongs to the DapB family.
CC       {ECO:0000256|ARBA:ARBA00006642}.
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DR   EMBL; KB630006; ERL83341.1; -; Genomic_DNA.
DR   STRING; 77166.U4TYH6; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000030742; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   CDD; cd01424; MGS_CPS_II; 1.
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; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   HAMAP; MF_00102; DapB; 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; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_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; IPR035686; CPSase_GATase1.
DR   InterPro; IPR022663; DapB_C.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR022664; DapB_N_CS.
DR   InterPro; IPR023940; DHDPR_bac.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR033937; MGS_CPS_CarB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   NCBIfam; TIGR00036; dapB; 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; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS01298; DAPB; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          760..955
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1306..1497
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1564..1701
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        524
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        608
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        610
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1701 AA;  184295 MW;  400B431B1A4D3886 CRC64;
     MSKADIRMAI AGSGGRMGRQ LIQAVQQAEG VVLGAALERK GSSLVGTDAG ELAGVGVANV
     IVSDSLEAVA EDFDILIDFT RPEGTLDHLS FCVKHGKGII IGTTGFDDAG KAAIKQAASD
     IPIVFAANFS VGVNVVLKLL EKAAKVMGDY TDIEIVEAHH RHKVDAPSGT ALAMGEAIAG
     ALGRDLKDCA VYAREGYTGE RDPMSIGFAT IRAGDIVGEH TAMFADIGER VEITHKASSR
     MTFANGAVRA GKWDALIKSA LLVLEDGTQF HGRAIGAEGT AIGEVVFNTS MTGYQEIITD
     PSYSRQIVTL TYPHIGNVGT NAADEESSAV HAQGLVIRDL PLIASNYRNE ETLSDYLKRH
     NIVSIADIDT RKLTRLLSEK GAQNGCIIAG DAIDAALALE KAKAFPGLKG MDLAKEVSTQ
     ESYSWQQGSW TLEGDLPEAK KAEDLPFHVV AYDYGVKRNI LRMLVDRGCR LTVVPAQTPA
     EDVLKLNPDG IFLSNGPGDP EPCDYAIEAI KTFLTTEIPV FGICLGHQLL ALASGAKTSK
     MKFGHHGGNH PVKNIDNNTV MITAQNHGFA VEEASLPATL RTTHKSLFDG TLQGLHRTDK
     PAFSFQGHPE ASPGPHDAAP LFDHFIELIE AYHIKSILIL GAGPIVIGQA CEFDYSGAQA
     CKALREEGYR VILVNSNPAT IMTDPEMADA TYIEPIHWEV VRKIIEKERP DAVLPTMGGQ
     TALNCALELE RQGVLAEFGV TMIGATADAI DKAEDRRRFD IAMKKIGLGT ARSGIAHNME
     EALVIAADVG FPCIIRPSFT MGGTGGGIAY NHEEFEEICT RGLDLSPTKE LLIDESLIGW
     KEYEMEVVRD KNDNCIIVCS IENFDAMGIH TGDSITVAPA QTLTDKEYQI MRNASLAVLR
     EIGVETGGSN VQFSVNPKDG RLIVIEMNPR VSRSSALASK ATGFPIAKVA AKLAVGYTLD
     ELMNDITGGK TPASFEPSID YVVTKIPRFN FEKFAGANDR LTTQMKSVGE VMAIGRTFQE
     SMQKALRGLE VGASGFDPIV NLEDPESLTK IRHELKDAGS DRIWYIADAF RAGMSLDAIF
     NLTNVDRWFL VQIEELVQLE GQVAQGGINA LDYGFLRVLK RKGFADLRLA KLAGVAESEI
     RKLRHSLNLH PVYKRVDTCA AEFSTDTAYM YSTYEEECES NPTNTKPKIM VLGGGPNRIG
     QGIEFDYCCV HASLALREDG FETIMVNCNP ETVSTDYDTS DRLYFESVTL EDVLEIVRIE
     KPKGVIVQYG GQTPLKLARE LEACGVPIIG TSPDAIDRAE DRERFQQAVI RLGLKQPANA
     TVATIEQAVE KAAGIGYPLV VRPSYVLGGR AMEIVYDEID MRRYFQNAVS VSNDAPVLLD
     RFLDDAVEVD VDVICDGERV LIGGIMEHIE QAGVHSGDSA CSLPAYTLSK EIQDVMRQQA
     EKLAFELSVR GLMNVQFAVK DNEVYLIEVN PRAARTVPFV SKATGVPLAK VAARVMAGQT
     LAQQGITEEV IPPYYSVKEV VLPFNKFPGV DPILGPEMRS TGEVMGVGRT FAEAFAKAQL
     GSLSTVKKTG RALLSVRDGD KARVVTLAGK LLEHGYEIDA TQGTAEVLTA AGITVRQVNK
     VHEGRPHIQD RIKNGEYAYI VNTTAGRQAI EDSKLIRRSA LQYKVHYDTT MNGGYATTMA
     LSSDPTEQVI SVQEMHAKIK A
//

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