ID A0A0D1ZFU6_9EURO Unreviewed; 2297 AA.
AC A0A0D1ZFU6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protein pyrABCN {ECO:0000313|EMBL:KIW11862.1};
GN ORFNames=PV08_09135 {ECO:0000313|EMBL:KIW11862.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW11862.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW11862.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW11862.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847498; KIW11862.1; -; Genomic_DNA.
DR RefSeq; XP_016232078.1; XM_016383455.1.
DR STRING; 91928.A0A0D1ZFU6; -.
DR GeneID; 27336218; -.
DR VEuPathDB; FungiDB:PV08_09135; -.
DR HOGENOM; CLU_000513_2_1_1; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000053328; 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; 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:UP000053328};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 626..818
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1162..1353
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1419..1571
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2297 AA; 252073 MW; 21F5247E18BE7D6F CRC64;
MVRTTPLTGD GRPSPSGTSL PQSPTVAASV GFPQMDRTIS ATPRLEGERM GSLIPIATAR
ASQEDEAKIY LELQDGQVFE GLSFGAPKSI SGELVFQTGM VGYPESVTDP SYRGQILVIT
FPLVGNYGVP SRETVDELLG NLPKHFESDL IHIGGLVVAS YAGEAYSHHL ATSSLGTWLK
EQGVPAMYGV DTRALTKIIR EEGSMLGRML YASTASQAKL SNGIRPDAQS NGEVMMGPVS
WREQVEPVEW HDQNKRNLVA EVSVKEPRVI SPPKSKALLH PSGRPVRVLV VDVGLKYNQL
RCLLARGVEV LVVPWDYNFP ELAGKDYDGL FISNGPGDPA MMSTTVKHIA AAMSEGRTPI
FGICLGHQLL ARAAGANTLK MKFGNRGHNI PCTNLLSGRC YITSQNHGFA VDSMTLPDGW
EELFVNANDG SNEGIRHVSR PYFSVQFHPE STPGPRDTEF LFDVFIDAIM KSVASVEALV
QPVSFPGGTI EENDKAHPRV QVKKVLVLGS GGLSIGQAGE FDYSGSQAIK ALKQEGIYTV
LINPNIATIQ TSKGLADKVY FLPVNADFVR KVIKHERPDG IYCTFGGQTA LQVGIQLKDE
FEGLGVRVLG TPIDTIITTE DRELFARSME SIGEKCAKSA SASSIEEAMH VVKDIGFPVI
VRAAYALGGL GSGFADNAEQ LRELCTKAFA ASPQVLIERS MKGWKEIEYE VVRDARDNCI
TVCNMENFDP LGIHTGDSIV VAPSQTLSDE DYNMLRTTAV NVIRHLGVVG ECNIQYALNP
FSKEYCIIEV NARLSRSSAL ASKATGYPLA FIAAKLGLNI PLNEISNSVT KKTCACFEPS
LDYVVVKIPR WDLKKFTRVS TQLGSSMKSV GEVMAIGRTF EEAIQKAIRS VDLHNLGFSD
ISNPLMSVDD ELQTPSDQRM FAIANAMHAG YSVDKIWEMT KIDKWFLSRL KGLSDFAKLM
SKYSTSTIPP SLFRQAKQLG FSDRQLARYW NSNELAVRLL RAEAGIHPVV KQIDTVAAEF
PAYTNYLYLT YNGMASDVTF EDHGIMVLGS GVYRIGSSVE FDWCSVRAIR TLRQEGYKTI
MCNDNPETVS TDYDEADKLY FENINLETVL DIHQLESANG VIISMGGQAP NNIALQLSRL
NIKILGTSPD MIDSAENRYK FSRMLDRINV DQPAWKELTS IEEALEFCAK VKYPVLVRPS
YVLSGAAMNT VYSKDDLASY LNQAVDVSRE HPVVITKYIE NAKEIEMDAV AKDGVMIGHF
ISEHVENAGV HSGDATLICP PQDLEPETIA RIEEATRKIG NALNVTGPFN IQFIAKDNEI
KVIECNVRAS RSFPFVSKVM GVDLIEMATK VMMGRPVTPY PPVDIPADYV GVKAPQFSFS
RLSGADPVLG VEMASTGEVA SFGRDRYEAY LKATISTGFK LPEKNILLSI GSFKDKMEML
PSVRKLHDMG YNLFATSGTA DFLEEHGIKV KYLEVLGSDE KEQKSEYSLT QHLANNKIDL
YINLPSSNRF RRPANYMSKG YRTRRMAVDY QTPLITNVKI AKILIEALAR HYDLSIHTID
FQTSHRTAVL PGLINVAAFV PGVAQTGSHD FSLVTKASIA AGFSMIRVMP VGIDSAITDV
RSLKIAQQNA EGGSYCDFNY SVAATDSNSE QIVHVKGEVG SLFIPFNHLA GNINKVATVT
AHFGTWPEYK PIVTDAKTTD LASILLLASL HGRKVHVMNV TSKDDISLIA LSKEKGLKVT
CDVSIYSLFL SQADYPDCPA LPTAVDQKAL WDHLSAIDVF SVGSIPYQIA GDHAVPTVGL
ADALPLLLTA VSEGKMTMED VTTRLHDNPK TIFELHDQNN TSIEVDINRP YVLQAGSAWS
PFVGKTLRGA ISRVIFQGKT ACLDGELSLD GPRGVDMSSH LLTPPTPAVG PTSPILRAQV
DASVDRRPTM FEATANRRVS TTVRSRPITR ARNMDEVLDD TNSPLLPTAA FRQPTAPSTI
SPSLLSLLAS SPFKNRHVLS VNQYTRQELH VLFTVAQEMR LGVQRQGIVP ILPSKVLCTM
FYEPSTRTSA SFDAAMQRLG GRTIAINTDH SSTQKGETLQ DSIRTLGCYG DAVVLRHPDN
ESAATAAKFS PVPIINGGNG SREHPTQAFL DLFTIREELG TVTGLTVTFT GDLKYGRTVH
SLVKLLQYYE VRINLVAPKD LALPEEVREQ IISSGQLAME SETLTPEIVA KSDVLYCTRV
QKERFTSLAE YERLKDSLIV DNSVLKYAKS TMVVMHPLPR NREISEEVDF DQRAAYFRQM
RYGLYTRMAL LALVLAS
//
