ID A0A135LVE4_PENPA Unreviewed; 2218 AA.
AC A0A135LVE4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATP-grasp fold, subdomain 1 {ECO:0000313|EMBL:KXG52909.1};
GN ORFNames=PGRI_081640 {ECO:0000313|EMBL:KXG52909.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG52909.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG52909.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG52909.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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}.
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:KXG52909.1}.
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DR EMBL; LHQR01000015; KXG52909.1; -; Genomic_DNA.
DR STRING; 5078.A0A135LVE4; -.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000070168; 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:UP000070168};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 567..759
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1102..1293
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1359..1509
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1837..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2218 AA; 243805 MW; BABB0C631908A069 CRC64;
MASVKGVIKP ACIPVRGGSD RLVSLELADG TVYQGYNFGA EKSVSGELVF QTGMVGYPES
ITDPSYRGQI LVVTFPLVGN YGVPSHDEMC ELLKDLPKHF ESSQIHIAAL VVASYAGEDF
SHFLAKSSLG DWLKSEGIPA MHGVDTRALT KHLRQTGSML GRMLLQKSGA SPEVAGTTGA
DWKSYFEETE WVDPNTKNLV AEVSIREPRL FTPPADVALK HPSGRGVRVL CLDVGMKYNQ
LRCLLARGVE VLVVPWDYDF PTLAGKDFDG LFVSNGPGDP ATLTVTTKNL AKMFEDARTP
VFGICLGHQL IARAVGAQTT KMKFGNRGHN IPCTSMLSGK CHITSQNHGY AVDSSSLQNG
WEELFVNAND GSNEGIRHTS RPFFSVQFHP ESTPGPRDTE YLFDVFINTI QSTIASPEAL
NLPVSFPGGT KAENVLAAPK VSVKKVLVLG SGGLSIGQAG EFDYSGSQAI KALKEEGIYT
ILINPNIATI QTSKGLADKV YFLPVNADFV RKVIKHERPD AIYVTFGGQT ALSVGIQLKD
EFEALGVKVL GTPIDTIITT EDRELFARSM DSINEKCAKS ASASTIEESL RVVEDIGFPV
IVRAAYALGG LGSGFAENMD QLKDLCTKAL AVSPQVLIER SMKGWKEIEY EVVRDAQDNC
ITVCNMENFD PLGIHTGDSI VVAPSQTLSD EDYNMLRTTA VNVIRHLGVV GECNIQYALN
PFSKEYCIIE VNARLSRSSA LASKATGYPL AFIAAKLGLG IPLNEIKNSV TQSTCACFEP
SLDYCVVKIP RWDLKKFTRV STQLGSSMKS VGEVMSIGRT FEEAIQKAIR MVDFHNLGFN
ESDALMSIKG ELQTPSDQRL FAIANAMAAG YTVDDIWKLT SIDKWFLTRL KGLSDFGKSI
SAFNATSVPM PMIRQAKQLG FCDRQLANFL DSNELAVRRM RVEAGITPIV KQIDTVAAEF
PAFTNYLYLT YNASQHDLSF DDHGIMVLGS GVYRIGSSVE FDWCSVRTIR TLREQGNKTI
MVNYNPETVS TDYDEADRLY FENINLETVL DIYQLETSSG VIMSMGGQTP NNIALPLHRL
NVNILGTSPE MIDGAENRYK FSRMLDRIEV DQPAWKELTS IDEARDFCEK VGYPVLVRPS
YVLSGAAMNT VYSEHDLASY LNQAVDVSRE HPVVITKYIE NAKEIEMDAV ARNGVMVGHF
ISEHVENAGV HSGDATLILP PQDLSPETVR RIEEATRKIG NALNVTGPYN IQFIAKDNDI
KVIECNVRAS RSFPFVSKVM GVDLIEMATK AMIGIPFQEY PPVSVPKDYV GVKVPQFSFS
RLSGADPVLG VEMASTGEVA SFGRDKYEAY LKALLSTGFR LPRRNILFSI GSYKEKLEML
PSIKKLHDLD YNLFATAGTA DFLKENGVPV KYLEHLPDHE EEDMKSEYSL TQHLSNNLID
LYINLPSNNR FRRPANYMSK GYRTRRMAVD YQTPLVTNVK NAKILIEAIA RHFPLNIIPS
DYQTSHRTVV LPGLVNIAAF VPNLVSAGSS DFETVSKASI GAGFSMIRVM PVGVDSSVTE
SRDLKIVQQN AHGKSLCDFN ISVAATATNS DQIIQMAGEV GSLFVPFNHL SGNINKVATV
TNHFSSWPSS KPLITDAKST DLASILLLAS LHSRNIHVMS VTSKEDISLI ALSKEKGLKV
TCDVSIYSLF LSREEFPACS SLPTAEDQKA LWEHLSTIDV FSIGSIPFQV AGKEATPESG
IAESIPLLFT AVSEGRLTIE DITARLCDNP KKIFELHDQV DSSLEIEIDR PYVFQNSQAW
SPFNGKTMRG SVQRVVFQGK TACLDGEITK DAVKGADMSS HRIVPTSPVQ KPMTPMARPE
SSLSRHVSMS GTPGRRFRAL DNAVPAIGEL GPPLYAPSSQ LSPSLADMLS RSPFRGKHIL
SVNQFSRADL HLLFTVAQEM RLGVQRHGVL DLLKGRVLTT LFYEPSTRTS ASFDAAMQRL
GGRTIAVATE HSSTQKGESL QDTIRTLGCY SDAVVLRHPE ASSTEVAAKY SQVPVINGGN
GALEHPTQAF LDLFTIREEL GTVTGLTITF TGDLKYGRPV HSLIKLLQFY DVRIQLVAPK
ALALPEDVRQ LIVASGQLVL ESEELTPEIV ASSDILYCTR VQKERFADLS EYERLKNTFV
IDNALLRHAK EHMVVMHPLP RNAEISEEVD FDQRAAYFRQ MRYGLYCRMA LLALVLAP
//
