ID A0A2P4ZAL6_9HYPO Unreviewed; 2228 AA.
AC A0A2P4ZAL6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Protein pyrABCN {ECO:0000313|EMBL:PON21358.1};
GN ORFNames=TGAM01_v209809 {ECO:0000313|EMBL:PON21358.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON21358.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON21358.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON21358.1,
RC ECO:0000313|Proteomes:UP000054821};
RX PubMed=26893428;
RA Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL Genome Announc. 4:e01747-15(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:PON21358.1}.
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DR EMBL; JPDN02000051; PON21358.1; -; Genomic_DNA.
DR STRING; 398673.A0A2P4ZAL6; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000054821; 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_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:UP000054821};
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..1502
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2228 AA; 244418 MW; 10815E6F8DA37CA2 CRC64;
MAVQLRKPAT ASHSGDERPV CLELEDGTIY QGFSFGAEKS IAGELVFQTG MVGYPESITD
PSYRGQILVI TFPLVGNYGV PSRETLDELL GDLPAHFESS QIHIAGLVTA SYCGEDFSHF
LATSSLGTWL KEQGVPAMYG VDTRALTKRI REKGSMLGKM RLASATATAD SLASLDAFEA
IDWVNPNTQN LVAQVSVKEP KLYKPPASVV ARQHPSGRTI RVLCVDVGMK FNQLRCFLKR
GVEVVVCPWD YDVTKATSEE YDGLFISNGP GDPAMLESTA KNIAAVMELN KIPIFGICLG
HQLMARAAGA KTTKMKFGNR GHNIPCTSMV TGKCHITSQN HGFAVDAGSL PTGWTELFVN
ANDGSNEGIM HVEKPYFSVQ FHPESTPGPR DTEYLFDVFI NTMASCAENS ALLQSPVSFP
GGAIEENERL HPRVSVKKVL VLGSGGLSIG QAGEFDYSGS QAIKALKEEG IYTVLINPNI
ATIQTSKGLA DKVYFLPVNA DFVRKVIQYE RPDAIYVTFG GQTALQVGIQ LKDEFESLGV
KVLGTPIDTI ITTEDRELFA RSMDSIGEKC AKSASANNVE EALHVVKDIG FPVIVRAAYA
LGGLGSGFAN NEQELTDLCH KAFAASPQVL IERSMKGWKE IEYEVVRDAQ DNCITVCNME
NFDPLGIHTG DSIVVAPSQT LSDEDYNMLR TTAVNVIRHL GVVGECNIQY ALNPFSREYC
IIEVNARLSR SSALASKATG YPLAFIAAKL GLGIPLKEIK NSVTKVTCAC FEPSLDYVVV
KMPRWDLKKF TRVSTQLGSS MKSVGEVMSI GRTFEEAIQK AIRAIDFHNL GFGETKALMS
IDDELQTPSD QRLFAIANAM HQGYSVDKIW EMTRIDKWFL RKLMGLSDFA KAMPQYSTAD
IALNPGILLQ AKRLGFSDRQ LAKFWSSNEI AVRRLRLEAG VQPFVKQIDT VAAEFPAFTN
YLYLTYNASE HDVDFDDHGV MVLGSGVYRI GSSVEFDWCS VRAIRTLRAT GHKTIMVNYN
PETVSTDYDE ADKLYFENIT LETILDIYQL ENASGVLGAM GGQTPNNIAL PLHRAGVKVL
GTSPEMIDTA ENRYKFSRML DRIEVDQPTW KELTSFEEAQ AFCQKVSYPV LVRPSYVLSG
AAMNTVYSEK DLESYLAQAA EVSREHPVVI TKYIENAKEI EMDAVAKDGV VVGHFISEHV
ENAGVHSGDA TLILPPQDLE RTTISRIEEA TRKIGAALNV TGPFNIQFIA KDNDIKVIEC
NVRASRSFPF VSKVMGVDLI EMATKAIMGQ PFQEYPPTDI APDCVGIKVP QFSFSRLSGA
DPVLGVEMAS TGEVACFGVD KNEAYLKALL STGFKIPKKN ILLSIGSFKD KKEMLPSVQK
LQKIGYKLFA TAGTADFLQE HGVPVQYLEV LGKEEDKDSE FSLTQHLSKN TIDLYINLPS
NNKYRRPANY MSRGYQTRRM AVDYQIPLVT NVKNAKILIE AIARSFDLSV SKRDYQTSHK
TVVLPGLVNV AAFVPGLVTP ESHDMETVTK ASISAGFSMI RVMPLGLEGA ITDGITLRAA
QQNSKLGDYC DYNLSVSATS DNDSQISTLA GEVGSLFIPF NHLSGNISKV AAVTAHFDAW
PAHKVIVTDA KLTDLASILL LASLHNRRIH VTSVTNKDDI RLIALSKAKG LRVSCDVSIY
SLYLSTKDYP ELDRLLPSPK DQAALWENMS TIDVFSVGSL PYQLAESLGK KADTSSGIAD
ALPLLLTSVT EGKLTIDDLK QKLYQNPMEI FELHDQVGTS IEVEIDRAYP VQPGSVWSPF
EGRLMRGSVR RVTFQDATVC LDGELLAVPP KGKDMSSHSI SREVPTSPAL KPAIGLITQV
TESPKPRQPA GFSSPKIAAR FRNLDGLGSP ARLGGAVDEL GLTLSPQPAT NSLQQLLSQP
NSFKNSHVLS VKQYTRSDLH LLFTVAQEMR LGVQREGVLN VLRGRVLCTL FYEPSTRTSA
SFDAAMQRLG GRTIAISTST SSVLKGETLQ DTLRTLACYG DAVVLRHPQE TSVDIANKYC
PVPVVNGGNG SKEHPTQAFL DLFTIREELG TVKGLTITFL GDLLYGRPVH SLVYLLQHYQ
VKVQLVSPKA LSLPAKVKEQ LIASGQLLVE SETLTPEILA RSDVLYCTRV QKERFESVEA
YEKVKDSYRV DNATLKNAKS SMVVLHPLPR NEEVAEEVDF DQRAAYFRQM RYGLYCRMAL
LALVMASS
//
