ID G8YKM2_PICSO Unreviewed; 2206 AA.
AC G8YKM2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Piso0_001378 protein {ECO:0000313|EMBL:CCE88606.1};
GN Name=Piso0_001378 {ECO:0000313|EMBL:CCE88606.1};
GN ORFNames=GNLVRS01_PISO0F05175g {ECO:0000313|EMBL:CCE88606.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE88606.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(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=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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
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 2nd section; belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00043998}.
CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily.
CC {ECO:0000256|ARBA:ARBA00043968}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
CC {ECO:0000256|ARBA:ARBA00043979}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00043984}.
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DR EMBL; FO082054; CCE88606.1; -; Genomic_DNA.
DR STRING; 559304.G8YKM2; -.
DR MEROPS; C26.956; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_1_1; -.
DR InParanoid; G8YKM2; -.
DR OMA; WSPFNGK; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000005222; Chromosome F.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000005222};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 556..748
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1094..1285
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1351..1502
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1827..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 296
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 380
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2206 AA; 244315 MW; 1119AA369EC95C1D CRC64;
MSSLSKPISP PMESTGNRMM TLQTHDGVAL QGYSFGAPVS AAGEVVFQTG MVGYPESITD
PSYEGQILVI TYPLVGNYGV PDRELKDDIV PQLPKYFESN KIHIAGLVVA HYTDEYSHFL
AKSSLGQWLK EQGVPAIYGV DTRNLTKRLR EKGSTLGRLA LQKDSVSSQT VLDACDWEKY
FDIPQWVDPN VDNLVAKVST KEPVLYTPSE NVKLGKDGKP IRILALDVGM KYNQIRCFVK
RGVELKVVPW DYDFSQEKYD GLFISNGPGD PSILKNVVTT LEKALKEVKT PIFGICLGHQ
LLARASGAST LKLKFGNRGH NIPCTSTISG RCYITSQNHG FAVDSSTLPS GWKELFVNAN
DGSNEGIYHE SKPIFSVQFH PESTPGPRDT EFLFDVFINS VVDFKSSGVY KPVEFPGGLL
EDNMAAHPRV EVKKVLVLGS GGLSIGQAGE FDYSGSQAIK ALKEEGIYTI LINPNIATIQ
TSKGLADKVY FLPVNPEFVR KVIKYERPDG IYCTFGGQTA LNVGIKLKDE FEDLGVKVLG
TPIDTVITTE DRELFARAMD TIDEKCAKSE AVNNVEEAID AANAIGYPLI IRAAYALGGL
GSGFADNEKE LVDLCNKAFA TSPQVLVERS MKGWKEIEYE VVRDAFDNCI TVCNMENFDP
LGIHTGDSIV VAPSQTLTDE DYNMLRTTAV NVIRHLGVVG ECNIQYALNP FSKEYCIIEV
NARLSRSSAL ASKATGYPLA YTAAKLGLNI PLNKITNSVT KSTCSCFEPS LDYVVVKIPR
WDLKKFTRVS SLLSSSMKSV GEVMSIGRTF EEAIQKAIRS TDYHNLGFNK TSALMSIDID
SELQTPSDQR LFAIANALSD GYSVDKVWKL TNIDKWFLNK LDGLIKFGNY ISSFGTKENL
PLTILKQAKQ LGFEDRQVAK FLNSNEVAIR RLRKEAGIIP FAKQIDTVAA EFPAYTNYLY
VTYNADSSDV DFDDHGVIVL GSGVYRIGSS VEFDWCAVRA IRTLRENKVK TVMINYNPET
VSTDYDEADR LYFETINLER VLDIYDLEQS QGVIVSMGGQ TSNNIALSLY RQNVKILGTS
PEMIDSAENR YKFSRMLDKI GVDQPAWKEL TSIEEAEEFA EKVTYPVLVR PSYVLSGAAM
NTVYSRADLA SYLTQAVDVS PDYPVVITKY IENAKEIEMD AVAKDGNMIM HVVSEHVENA
GVHSGDATLI VPPQDLDPET VRRIVEATAK IGKALDITGP YNIQFIAKDN DIKVIECNVR
ASRSCPFVSK VVGTDLIELA TKAMMDLPFK PYPGQKLPDN YCALKVPQFS FSRLAGADPV
LGVEMASTGE VATFGRNKYE AYLKSLMSTG FKLPKKNVLF SIGSYKEKQE LLPAIRKLYE
CGYKIFATAG TADFIKEHSI PVHYLEVLKK EDDQKSEYSL TQHLANNLID LYVNLPSANR
FRRPASYMSK GYESRRMAVD YSVPLVTNVK CAKLLVEALT RDISLEVSNN DAQTSHETAI
IPGLINIASF IPSFDDFESA TRASLVSGFT YNAFLPQTAE GCTVVDSESL SNAISNATEF
AYTDFSISIA ALETNADGIE EAASNAGALF IPFNEFSSSK VSSISKHFAS WPANKPIITD
AKSTNLASVL LLAALHNRTL HVNSVSSKED LDLIKMAKEK ALQVTCDVAV YSLFLSQEQY
PELELLPTKS DQEYLWANLK DIDCFSIGVL PYLIAKSIHQ RLVPGLGVTE TLPLLFSAVK
AGKLTIQEIT EKFHDNPMKI FNFPKQDASI EIDLDRLIPS TRKLGLSPFD RKQLQGSVNR
VSFHNQTVCL DGEIVAQQAV GKHEVGNKGR SLSMVQQSPT LGRKSRLSFS EATAPSLKRE
KNQSPAVFEK LGSKLVSEPP TDALADSNAL ANYIRNNNPF LRNSVLSVAE FTRSDLHSLF
TVAQEMRLAV ERSGVLDILK GRLLATMFYE PSTRTSTSFD AAMQRLGGRV VPVSIASSSV
KKGETLQDTI RTLACYSDAI VLRHPEEASA DIAAKYSPVP IINGGNGSKE HPTQALLDLF
TIREELGTVN GITVTFMGDL KYGRPVHSLC HLLRLYQVRV QLISPKELNM PENIRKMLTE
NGMLMYESDK LTEDVIAKSD VLYCTRVQEE RFADKEQYHR LKDSYIVDNK ILSYAKQHMC
VMHPLPRTSE IREEVDFDQR AAYFRQMKYG LYVRMALLAM VIGIDF
//
