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Database: UniProt
Entry: A8PXN5_MALGO
LinkDB: A8PXN5_MALGO
Original site: A8PXN5_MALGO 
ID   A8PXN5_MALGO            Unreviewed;      2217 AA.
AC   A8PXN5;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   13-SEP-2023, entry version 90.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDP44092.1};
GN   ORFNames=MGL_1489 {ECO:0000313|EMBL:EDP44092.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44092.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP44092.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP44092.1}.
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DR   EMBL; AAYY01000004; EDP44092.1; -; Genomic_DNA.
DR   RefSeq; XP_001731306.1; XM_001731254.1.
DR   STRING; 425265.A8PXN5; -.
DR   MEROPS; C26.956; -.
DR   GeneID; 5855613; -.
DR   KEGG; mgl:MGL_1489; -.
DR   VEuPathDB; FungiDB:MGL_1489; -.
DR   InParanoid; A8PXN5; -.
DR   OMA; FTGDLRY; -.
DR   OrthoDB; 309at2759; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008837; 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   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   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:UP000008837};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          530..722
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1049..1240
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1306..1456
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        346
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   2217 AA;  242372 MW;  E41D503CB8F8C0DE CRC64;
     MVGYVESLTD PSYEGQILVL TYPMVGNYGV PARPTDAAAM TQVPPKLQAP FESTRIHVAG
     LVVAYYSHDF SHYLAASGLS DWLKENGVPA VYGIDTRALT KRIRTKGSML ARLLAARPGA
     SLGGDWREQV LDVPWHNPNG ENLVAKVSCK MPMLYTPQDT APAGLRMANE PTLMHTSGRP
     IRVLALDVGM KQNQIRCFTS RGVELKVVPF DHDILTEPEP YDGLFISNGP GDPMQCTQTI
     QRLRALLART SDVIPIFGIC LGHQLLALAA GAQTTKMKYG NRGQNIPCTS QLSGRCYITS
     QNHGYAVDAQ SLPDGWAELF VNANDHSNEG IYCTHAPFFS VQFHPESTPG PRDTEFLFDV
     FVRSVVDNAA VRHSAHSGGN ALTLAPVAFP GGRRADHEAA FPRLHPKKVL VLGSGGLSIG
     QAGEFDYSGS QAIKALKEEG IYTVLINPNI ATIQTSAGLA DKVYFLPVTP EFVLKVLRHE
     RPDGIYCTFG GQTALNVGIH LKDEFEKLGV LNLGTPIDTI IKTEDRDLFA RAMEEIGERC
     APSASANTWD EALQAAHNIG FPVIVRAAFA LGGLGSGFAK NEDELRRLCH TAFANSPQVL
     VEKSMRGWKE VEYEVVRDCR DNCITVCNME NFDPLGVHTG DSIVVAPSQT LSDEDYNMLR
     TTAVNVIRHL GVVGECNIQY ALNPHSREYC IIEVNARLSR SSALASKATG YPLAFVAAKL
     GLNIPLNELR NSVTRETCAC FEPSLDYVVT KIPRWDLRKF MRVSSKLGSS MKSVGEVMAI
     GRTFEESVQK AIRSVDPSFA GFSENDMVDD AEIDEELEFP TDRRIFAVAN ALARGRSVEH
     IHKLSNIDRW FLRKLEGIIA AAKAMEHSGA AQIPADLLRR AKQLGFSDHQ IAKYSASTEL
     AVRRRRQELG ITPFVKQIDT VAAEFPAQTN YLYTTYHAVE HDLNFEDHGV MVLGSGVYRI
     GSGFKTVMVN YNPETVSTDY DEADRLYFEN ISLETVMDIY EMEQSTGVVI SMGGQTPNNI
     ALPLHRQGVK ILGTSPEMID NAENRYKFSR MLDRLGVDQP MWKELSSFED AHNACARFGY
     PVLVRPSYVL SGAAMNVVYS AEDLSSYLSQ ATAVNREHPV VITKYLEGAK EIEMDAVAKD
     GKLIMHYVSE HVENAGVHSG DATLILPPQD LEIETVRRIE HATSMIVEAL NVTGPCNIQF
     IAKNNEIKVI ECNVRAARSF PFVSKVTNVD AIEMATCAMM GLPVEPYPQV DLPKDYVGVK
     VPQFSFSRLS GADPILGVEM ASTGEVACFG RNKYEAYLRA LLASGIRMPT NNVLLSVGPF
     SEKQELLPSV RTLHQLGFTL YGSSGTADFY SENGIPVIHL EALPEDEDWR GDESSKASYS
     LLTHLTQGRS SLFISLPSKN KYRRPSSFTS MGYRARRLAI DRSIPLVTNV KNAKLFVEAL
     AVHRRLGNSF DILPVDAKTS HKTCTFPGFV ELQAFVPSMG AALTKQHVAE YTRAAARGGF
     TSIVCSPVGS VGSDSSTMSA IVDEESLSAA EAALDGQCCV DVSLTLLATP EHVGELPHLS
     SRVRALFVSY SGSAREHSLR PANVANYFAH WPEDKLILTD ACGADLASVL LLASLHNRPL
     HVTNVRCSDD VQLIALSKAK GLRVTCDVPV HALFFSNDMY PMASCLPSAQ DQAALWDHIE
     DIDAFSMGPV PWELATQVGH EPLPTIGTDD AVRMLLNAVN EGRLTIDHIT SRLGTNPRMI
     FQLPEQPETH VFAEIDRIEH HHQHHDQDGR PAWSPLDTAS LRGTINRVEL RGKTLMLDGK
     LRANVPLGSN VSALEQPRIS TGAAPAASST VGGAAASTMA GGAASSGVAG TGLSGLDVPV
     SPSIALRSPR RRPLVAGATR QPSQIDELRL EPVAGPAPVT RLSLYHGSFS RRHILSVRQF
     TRDDLHALFA VAQEMRFLVQ RNGTLDVLRG HILCTLFYEE STRTSASFEA AMLRCGGQVV
     SINTSRSSVA KGETLADTVR TLGCYGDAVV LRHPAVGSSQ EAAKFSPVPV INAGDGVGEH
     PTQALLDVFT IREELGTVNG LTVTLLGDLK NGRTTHSLVR LLSHYGVRVN FVSPPSLAMP
     REVIREVVKH GMAVYETSNL DEVIGTTDVL YVTRIQRERF ASQDEYEAVK GCYVVNNDVL
     ARAKPDLAVL HPLPRVDEID PEVDFDIKRA AYFRQMRCGL YIRMALLAMV MQSSDRS
//
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