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
//