ID Q6FL72_CANGA Unreviewed; 2211 AA.
AC Q6FL72;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE SubName: Full=Candida glabrata strain CBS138 chromosome L complete sequence {ECO:0000313|EMBL:CAG61992.1};
GN OrderedLocusNames=CAGL0L05676g {ECO:0000313|CGD:CAL0135348,
GN ECO:0000313|EMBL:CAG61992.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG61992.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG61992.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380958; CAG61992.1; -; Genomic_DNA.
DR RefSeq; XP_449022.1; XM_449022.1.
DR STRING; 284593.Q6FL72; -.
DR MEROPS; C26.956; -.
DR EnsemblFungi; CAGL0L05676g-T; CAGL0L05676g-T-p1; CAGL0L05676g.
DR GeneID; 2890801; -.
DR KEGG; cgr:CAGL0L05676g; -.
DR CGD; CAL0135348; CAGL0L05676g.
DR VEuPathDB; FungiDB:CAGL0L05676g; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_1_1; -.
DR InParanoid; Q6FL72; -.
DR OMA; WSPFNGK; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0016020; C:membrane; IEA:EnsemblFungi.
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:EnsemblFungi.
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 GO; GO:0045984; P:negative regulation of pyrimidine nucleobase metabolic process; IEA:EnsemblFungi.
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:UP000002428};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 560..752
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1097..1288
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1354..1505
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2211 AA; 244803 MW; 90B5BCB721516E27 CRC64;
MTTPVAPITP PMETTGDRLV TLELKDGTTL QGYSFGAEKP VAGELVFQTG MVGYPESITD
PSYEGQILVI TYPLVGNYGV PDFNLRDEFI ESLPRYFESN RIHVAGLVIS HYTEDYSHYL
AESSLGQWLK REGVPAVYGI DTRALTKHLR NCGSMLGRLA LQEASAKLEV ATSESWKSVF
DVPEWVNPNV ENLVAKVSLK EPKLFTPPSD NKYVEVKKGA DGKTIRILAI DVGMKYNQIR
CFVKRGVELL VVPWDYDFTK EDYDGLFISN GPGDPSVLND LANRLSKALE KKKTPIFGIC
LGHQLLARAS GASTLKLKFG NRGHNIPCTS TISGRCYITS QNHGYAVDVD TLTPGWKPLF
VNANDDSNEG IYHTELPYFS VQFHPESTPG PRDTEFLFDV FINAVLEHKN SGVLKPVEFP
GGKIENNRKE NPRVEAKKVL VLGSGGLSIG QAGEFDYSGS QAIKALKEEG IYTILINPNI
ATIQTSKGLA DKVYFLPVTA EFVRKVILHE RPDAIYVTFG GQTALSVGIE MKDEFESLGV
KVLGTPIDTI ITTEDRELFA NAIDEIDEKC AKSQAANSVE EALAAVKDIG FPVIVRAAYA
LGGLGSGFAN NEQELIDLCN VAFASSPQVL VERSMKGWKE VEYEVVRDAF DNCITVCNME
NFDPLGIHTG DSIVVAPSQT LSDEDYNMLR TTAVNVIRHL GVVGECNIQY ALNPFSKEYC
IIEVNARLSR SSALASKATG YPLAYTAAKL GLNIPLNEVK NSVTKSTCAC FEPSLDYCVV
KMPRWDLKKF TRVSTELSSS MKSVGEVMSI GRTFEEAIQK AIRSTEYSNL GFNATDLEID
IDYELQNPSD LRIFAIANAF DKLGYSVEKV WEMTNIDKWF LNKLYDLVKF ASKVSSCGGI
EGLSPTVLRQ AKQLGFDDRQ IASFTSSNEV AIRRLRKDYG IIPFVKQIDT VAAEFPAYTN
YLYMTYNAAE HDVEFNDHGV MVLGSGVYRI GSSVEFDWCA VTAVRTLRAN NIKTIMINYN
PETVSTDYDE ADRLYFETIN LERVLDIYEA EASNGVVVSM GGQTSNNIAM SLHRENVKIL
GTSPDMIDSA ENRYKFSRML DQIGVDQPAW KELTSMDEAE DFAEKVGYPV LVRPSYVLSG
AAMNTVYSKN DLESYLNQAV EVSRDYPVVI TKYIENAKEI EMDAVARNGE LVMHVVSEHV
ENAGVHSGDA TLIVPPQDLA PETVDRIVVA TAKIGKALKI TGPYNIQFIA KDNEIKVIEC
NVRASRSFPF ISKVVGVNLI ELATKAIMGL PFAPYPVEKL PDDYVAVKVP QFSFPRLAGA
DPVLGVEMAS TGEVATFGHS KHEAYLKSLL ATGFKLPKKN ILLSVGSYKE KIELLPSVQK
LYNMGYKLFA TAGTADFLTE HGLSVQYLEV LNEDEPEKKE YSLTQHLANN EIDLYINLPS
ANRFRRPASY VSKGYRTRRM AVDYSVPLVT NVKCAKLLVE ALAQNISLNV SERDAQTSHR
TVTIPGLINI TTYVPNITNV VEGPAELKET TRLFLESGFS YCQIMPRASR GPVINDAASI
KVATSVSNNS CHTDFAFTIA GTAHNAQQIA QSADKANALY LPLHELKNKV STISELLSNW
PSNKQVITEA KTSDLASVLL LASLQNRSIH ITGVSKKEDL SLIMTVKEKD PKVTCDINVY
SLFVTQEQWP EAMFLPTEED QEFFWKNLSA IDAFSIGSVP TQLAEITGNK VEVGLGIKDA
LPLLLSAVEE GKLTVDDIVE KLHDNPAKIF NIPTQNSLVE LDLDFSFASK KRWTPHSNTS
LRGGIERVVV NDETLVLSGE LVATEPKGTL KMKSELVQAS VENAPAIQST GRRMTIHDDK
LMDVDSAENS IPDAPIQQKL MSSKPPRELT APSALQNLIR GNNPFQGRHI LSIKQFSRAD
FHALFAVAQE LRAAVAREGV LDLMKGHIIT TIFYEPSTRT CSSFIAAMER LGGRVVNINP
NVSSVKKGET LQDTIRTLAC YTDAIVMRHS EEMSVHIAAK YSPVPIINGG NGSREHPTQA
FLDLFTIREE IGTVNGITVT FMGDLKHGRT VHSLCRLLMH YQIRINLVSP PELRLPESLR
EELNSKGQLG VESVALTPEI ISKSDVLYCT RVQEERFKST EEYERLKDFY IVDNKILSHA
KQNMAVMHPL PRVNEIKEEV DYDHRAAYFR EMKYGLYVRM ALLAMVLGVN N
//
