UniProt: M4B1H1

Database: UniProt
Entry: M4B1H1_HYAAE

LinkDB:  M4B1H1_HYAAE 
Original site:  M4B1H1_HYAAE

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (29)   
   InterPro (16)   
   Pfam (5)   
   PROSITE (5)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (37)   

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ID   M4B1H1_HYAAE            Unreviewed;      1517 AA.
AC   M4B1H1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=carbamoyl-phosphate synthase (ammonia) {ECO:0000256|ARBA:ARBA00044063};
DE            EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP800118, ECO:0000313|Proteomes:UP000011713};
RN   [1] {ECO:0000313|Proteomes:UP000011713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA   Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA   Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA   Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA   Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA   Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA   Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA   Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT   arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [2] {ECO:0000313|EnsemblProtists:HpaP800118}
RP   IDENTIFICATION.
RC   STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP800118};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
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; JH597776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 559515.M4B1H1; -.
DR   EnsemblProtists; HpaT800118; HpaP800118; HpaG800118.
DR   VEuPathDB; FungiDB:HpaG800118; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_000513_0_1_1; -.
DR   InParanoid; M4B1H1; -.
DR   OMA; FPFNKFP; -.
DR   Proteomes; UP000011713; 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:UniProtKB-UniRule.
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   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; 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};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          559..751
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..1517
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        301
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1517 AA;  167229 MW;  4947B2DE3A8FA7CF CRC64;
     MLRVAQSVVK TRRVPLYKAS GHRLLVSARE KAVKVDRRNV PRFETPAVLE FEDGSRFHGV
     SFGAKKSMAG EVVFTTGMVG YPEALTDPSF KGQLLNMTFP MIGNYGVPDT TALDDIGLHK
     YIESDRIHAA GVIVQDYSSH YSHWNAAQSL SEWLENEGIP GIAGVDTRAI TKKIRAHGAM
     AGRILIDGCS DTPHLVDVNE TNLASLVSTK KVVTYGKGNP LKILAVDCGI KYNIIRELVN
     RGAEVKRVPW NHDISSEIGW YDGLFISNGP GNPAIMKETT AQLRKAMALQ GDNVKPIFGI
     CLGNQLLSLA AGAKTYKLPY GNRGQNQPVH NLKTGRCYIT AQNHGFAVDG KTLPSEWEEL
     FVNLNDGTNE GIIHKSKPYF TAQFHPEHAG GPTDTQFLFD TFLDAVRVKE KGPIKSLVQR
     PDVKRVKVKK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE ENIETILINP NIASVQTNID
     RSSEAQASNV YYLPVNPDFV EQVIKRERPD GILISMGGQT ALNCGMELDK RGVFKKYDVK
     VLGTQIEVIN YTEDRELFNG KLAEINECIA QSEAVESVDA AVKAAYKIGF PVMIRSAFAL
     GGLGSGICDD EAHLRTMAKQ AFSGSPQILV ERSMKGWKEV EYEVVRDAAD NCLTVCNMEN
     FDPLGIHTGE SIVIAPSQTL SNNEYHILRE TALKVVRHLG IVGECNIQYA LNPESEEYCI
     IEVNARLSRS SALASKATGY PLAFVAAKLA LGMNLPDLKN SVTKSTTACF EPSLDYCVAK
     MPRWDLAKFE NVSTEIGSSM KSVGEVMSIA RTFEEAIQKA IRMVEPSNEG FEPRYDELSH
     EELVKALGKP TDRRIYQIAQ ALKTGQLSIE QVHEITKIDT WFLSRLQAIC DCDVNLTGKK
     LHEITGPEIV NAKKLGFSDR QLARMFSCSD DEVRAKRKEL GIVPSVKQID TLAAEYPAQT
     NYLYMTYNGT EHDVPALEPN DGVMVLGSGA YRIGSSVEFD WCAVSCIRTL RKLGHRAVML
     NYNPETVSTD YDECDQLYFE ELSKERVMDV NDREGVRGVV VSVGGQIPNN LALPLHKAGV
     KILGTHPTMI DSAEDRFKFS KLMDAAGVPQ PAWKELTNHT DAREFAERVG YPVLVRPSYV
     LSGAAMNVAY NFEELENVLN QAVAVSAEHP VVITKFVEGA KELELDAVAR NGKVIAAAIS
     EHVENAGVHS GDATLVLPPV EASAFYTNQI KRNAEKIAKA LNISGPFNAQ FLAKGAEVSV
     IECNLRASRS FPFVSKTTGA DFVNAATKVM VGESTDNDNL PALYGPKRPE GFVGIKSPMF
     SYTRLGGADP LLGVEMASTG EVACFGKNRH EAFLKALISS NIKLPEKNIL LSMQDKFSED
     FVHAAYQMHE LGYKLYTTKK THAYLKKYDI PSTEVDFPLD ADSENNVLNL IRDGKIDLVV
     NLPNNESQQT KNNYLIRRTA VDFSIPLLTN ISLVQLFVEA MAVHKNQPLL GLEPDSLFDY
     YEREKKDEVW TDEHEFH
//

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