ID R0LH83_ANAPL Unreviewed; 1507 AA.
AC R0LH83;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=carbamoyl-phosphate synthase (ammonia) {ECO:0000256|ARBA:ARBA00044063};
DE EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
DE Flags: Fragment;
GN ORFNames=Anapl_06329 {ECO:0000313|EMBL:EOA99672.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA99672.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB743291; EOA99672.1; -; Genomic_DNA.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 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; 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 HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR017926; GATASE.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 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; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
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; SSF52335; Methylglyoxal synthase-like; 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; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 558..750
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1100..1291
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1362..1507
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA99672.1"
FT NON_TER 1507
FT /evidence="ECO:0000313|EMBL:EOA99672.1"
SQ SEQUENCE 1507 AA; 164988 MW; 776DB248A588B174 CRC64;
YPSATLKMTR ILTACKVVKT LKGRLEFCKV SADHWSFSRT GTRLLSIKAQ TANLVLKDGT
KMKGYSFGYP SSTAGEVVFN TGISGYTEAL TDPSYKGQIL TLANPIVGNS GVPDTAALDE
MGLRRFLESD GIKVSGLLVL DYSNEYSHWQ ATRSLGEWLQ EEKVPALYGI DTRMLSKLIR
DKGTVLGKIE FEGQPTEFAD PNKQNLIAEV STKEVKVYGR GNPIKVVAVD CGLKYNVIRL
LVKRGAEVQL VPWDHDFTSM DYDGLVISGG PGDPMKAQEV IQNVRKVLES NRPEPLFGIS
MGHVITGIAA GATSYKMQMA NRGQNQPVLN AVNGQAVITA QNHGYAIDSS TLPPGWKPLF
VNANDQTNEG IMHETRPIFT AQFYPDANPG PTDTEFLFDS FISLVKRGKG TTVASVLPKA
GAAASRVEVS KVLILGSGGL SIGQAGEFDY SGSQAVKAMK EENVKTVLMN PNIASVQTNE
TGIKQADAVY FLPITPHFVT EVIKAERPDG LILGMGGQTA LNCGVELFKQ GVLQQYGVKV
LGTSVESIMA TEDRKLFSDK LTELNEMIAP SFAVESIEDA LKAAEKISYP VMIRSAYALG
GLGSGICPDE ESLLDLGTKA FAMTNQILVE KSVVGWKEIE YEVVRDAADN CIAVCSMENI
DAMGVHTGDS VVVAPSQTLA NEEFQMLRDR AIKVVRHLDI VGECNIQFAL HPTSLEYYII
EVNARLSRSS ALASKATGYP LAFIAAKIAL GIPLPEIKNV MTGNTSACFE PSLDYVVTKI
PRWDLDRFQG TSNRIGSSMK SVGEVMAIGR TFEESFQKAL RMCHPSVDGF TSRLPLNKAW
PASTDLQKEL SEPSSTRIYA IAKALTNKVP VDVIHKLTAI DKWFLYKMRG IVNMEKILKE
ANSEAVPEET LRRAKQLGFS DKQVGKCLGL TELQCRQLRL RKNIAPWVKK IDTLAAEYPA
VTNYLYVTYS GQEHDVKFDD CGVMVLGCGP YHIGSSVEFD WCAVSSIRTL RQLGNKTVVV
NCNPETVSTD FDECDRLYFE ELSLERILDI YQYEGCSGCI ISVGGQIPNN LAVPLYQSGV
KILGTNPLQI DRAEDRSVFS AVLDELRVAQ APWKAVSTLR DAVEFAGSVS YPCLLRPSYV
LSGSAMNVVF TEDEMKKFLA EATRVSQDHP VVLTKFIEDA REVEMDAVAK AGRVISHAIS
EHVEDAGVHS GDATLMLPTQ TISQGALEKV KAATKKIANA FAISGPFNIQ FLVRGNDVLV
IECNLRASRS FPFVSKTLGV DFIDVATKVM IGKEVNESTL PTLEQPIIPS KYIGIKAPMF
SWTRLRDADP VLRCEMASTG EVACFGEDVY SAFQKAMLAT GFTFPKKGIL IGIQKSFRPK
FLSVAELLCE EGFELYATEA TSDWLNANSI SANPVAWPSQ ESQNPSLPSV RRLIRDGKID
LVINLSNSNT KFVHDNYMIR RMAIDSGIAL LTNFQVTKLF AEAVKYSGKL DSKSLFHYRQ
FDNGNAA
//
