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
//