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Database: UniProt
Entry: I4YEY0_WALMC
LinkDB: I4YEY0_WALMC
Original site: I4YEY0_WALMC 
ID   I4YEY0_WALMC            Unreviewed;      2260 AA.
AC   I4YEY0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Carbamoyl-phosphate synth {ECO:0000313|EMBL:EIM22522.1};
GN   ORFNames=WALSEDRAFT_31765 {ECO:0000313|EMBL:EIM22522.1};
OS   Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS   633.66)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM22522.1, ECO:0000313|Proteomes:UP000005242};
RN   [1] {ECO:0000313|EMBL:EIM22522.1, ECO:0000313|Proteomes:UP000005242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX   PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA   Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA   Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA   Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA   Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT   "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT   osmotic stress and suggests cryptic sexual reproduction.";
RL   Fungal Genet. Biol. 49:217-226(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001363};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852}.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC       hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008454}.
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DR   EMBL; JH668227; EIM22522.1; -; Genomic_DNA.
DR   RefSeq; XP_006957194.1; XM_006957132.1.
DR   STRING; 671144.I4YEY0; -.
DR   GeneID; 18471365; -.
DR   KEGG; wse:WALSEDRAFT_31765; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_000513_2_0_1; -.
DR   InParanoid; I4YEY0; -.
DR   OMA; FTGDLRY; -.
DR   OrthoDB; 309at2759; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000005242; Unassembled WGS sequence.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
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:InterPro.
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: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; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
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; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   NCBIfam; TIGR01368; CPSaseIIsmall; 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; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
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; SSF53671; Aspartate/ornithine carbamoyltransferase; 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; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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:UP000005242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          613..805
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1151..1342
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1408..1556
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1891..1930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        354
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   2260 AA;  247616 MW;  CD35EF2D78B66B26 CRC64;
     MSGAPSPPSN PLELAPSQPP AAHALAKQST VRNNNGILYP ATAQPAGVES DYDTALELED
     GSVNFGYSFG AKGKSISGEC VFQTGMVGYP ESLTDPSYAG QILVLTYPLV GNYGVPARPA
     ETNPLNLPEE FESAKIHVAG LVVSTYAPDY SHFLANSSLG TWLQEQGIPA VFGVDTRNLT
     KKIREKGVML GRILARKNGD RSGRPLLSQP AASLSRSVST ASMGSAVVND SWKEDFQVIP
     FTEYGNTNLV AQVSLPTPLI FKPTATPLKH PKEDRNVRIL TVDVGIKYNQ IRCFNNRGVE
     VKLVPWDYDF LNESEPYDGL FVSNGPGDPA TVTPVIEKLR TAVDQTKTPI FGICLGHQLL
     SLAVGAKTKK MKYGNRGANI PCTDMQSGRC YITSQNHGYA VDADTLPEGV KELFVNANDG
     SNEGTYLEDK PVFSVQFHPE STPGPRDTEF LFDVFINSVV DFAKTGVKKQ IVLPGGTLAD
     NAAKYPRVDV KKVLVLGSGG LSIGQAGEFD YSGSQAIKAL KQEGIYTVLV NPNIATIQTS
     GLADKVYFLP VNPDSVRKII KHERPDGIYV TFGGQTALNV GCKLKDEFEA LGVKVLGTPV
     NTIEMTEDRE LFARAMEEIG EHCAPSASAN SLDEALQAAK NIGYPVIARA AYTLGGLGSG
     FADDEKSLTQ LCNKAFATSP QVLIEKSMKG WKEIEYEVVR DCRDNCITVC NMENFDPLGI
     HTGDSIVVAP SQTLSDADYN MLRSTAVKVI RHLGVVGECN IQYALNPHSK EYCIIEVNAR
     LSRSSALASK ATGYPLAYTA AKLGLNIPLN EIRNSVTRST TACFEPSLDY CVVKIPRWDL
     KKFNRVNTAL NSSMKSVGEV MAIGRSFEET IQKAIRCIDD RFYGFGTNPF VMEKAEIDEE
     LVNPTDRRVF AIANAFVKGY TVDQIHKMSN IDRWFLNRLK NLIEQEKILS EFNTTNVTPQ
     LLRQSKQMGF SDRQLAKFLG SNELAVRRLR QESGIVPHVK QIDTVAAEFP AFTNYLYTTY
     NAGASDIDFE DKGVIVLGSG VYRIGSSVEF DWCAVSTIRT LRSRGVKTVM INYNPETVST
     DYDEADRLYF ENISLETVLD IYDAERSTGV ILSMGGQTPN NIALPLYRQN VHIYGTSPEM
     IDTAENRYKF SRMLDKIGVD QPQWKELSSF DEAYKFCQNV GFPVLVRPSY VLSGAAMNVV
     SSPDDLENYL TQATAVSQDY PVVISKFIED AKEIEMDAIA KDGKMIMHYI SEHIENAGVH
     SGDATLVLPP QDLAPETVRR IVEATAKIGE ALNVTGPYNI QFIAKNNEIK VIECNLRAAR
     SFPFVSKVTN VDAIALATNA MLGFTFTPYP EISLPEKYVG VKVPQFSFSR LSGADPVLGV
     EMASTGEVAC FGRDKYEAYI KALMATGMHM PKKNILFSIG SYKEKMEMLP AVQNLHRQGY
     NLFATSGTAD FIQEHGIPVK YLEAITETDS QKSEYSLTQH LANNLIDLYI NLPSKNRYRR
     PASYMSKGYQ SRRMAVDYAV PLVTNVKCAK LLIEAIVRKP SLEVDSVDYK TSHRTFTLPG
     LINVQAYTDK VAEANSGSFE KATLAALEGG FTVAQVIPMG VENGKSLQAM HTNAVKSRCD
     YVLSVSATPD NVDGLDAFEE DVQSLYIPFN KLSGNVNKVA TIASHFGSWP SGKPIVTDAR
     STDLASILLL ASLHGRSIHV TNVSNRDDIS LIALSKGRDL KVTCDVAVYS LFFSREDYPE
     ATVLPTKKDQ KALWDNLDKI DMFSVGTVPH ELAVAVGQGA NASAGMAESV SLLLSAVAEQ
     KLTLEDVISR FHDAPKAIFD LPDQPNTYVE VEMDRASSFS ASEGLWSPLN GKPVKGQVDR
     VVFYGKTVRL AGVNVSKSTG RDLTVAGPIR KQRNARTSFS QQTRPATQSI TGIPSPTKNK
     DGLSSPVDGT QPRSFMSALD PLSTGKGDLT ALKSHPAFKR RHILSVKQFT RDDLHVLFTL
     ASELRTHVEK YGSADILKGR VLCSLFFEPS TRTSASFDAA MKRCGGTVVT IPVDRSSVAK
     GESLADTIRT LGCYADGVVM RHPVPGSVQT ASKFSPVPII NAGDGTGEHP TQAFLDIYTI
     REELGTVNGL TITMVGDLKN GRTVHSLVKL LNLYNVHLNF VSPPSLNMPD SIKAECRKSG
     VTFHETARLD DVIGKSDVIY MTRVQQERFN SVHEFEAVKD AYILDNATMD KAKPSTIVLH
     PLPRLQEIDP NLDFDNRAAY FRQMRYGLFA RMALLSLILE
//
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