ID A0A167DQW8_9PEZI Unreviewed; 2233 AA.
AC A0A167DQW8;
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=Protein pyrabcn {ECO:0000313|EMBL:KZL84219.1};
GN ORFNames=CI238_12737 {ECO:0000313|EMBL:KZL84219.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL84219.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL84219.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL84219.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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}.
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:KZL84219.1}.
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DR EMBL; LFIW01000933; KZL84219.1; -; Genomic_DNA.
DR STRING; 1573173.A0A167DQW8; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000076584; 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:UP000076584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 571..763
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1108..1299
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1365..1544
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1861..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2233 AA; 245302 MW; 2D48B8287ABC25EB CRC64;
MVATVYPPAA ARIVGSDDEG LMALEMPDGS VYQGYSFGAQ KSIAGELVFQ TGMVGYPESV
TDPSYRGQIL VITFPLVGNY GVPSRETVDE LLGDLPAHFE SSQIHIAGLV AHSYSGEDYS
HFLAESSLGT WLKEQGVPAI YGVDTRALTK RLRSQGSTLG RLLLQKKTLT NGTANGHVNG
VASFSLDDFQ TVDWVNPNEK NLVAEVSIKA PKLYKPPASV AVKKHPSGRP IRVLCLDVGM
KYNQLRCFLK RGVEVLVCPW DHDLVKQAGE EYDGLFLSNG PGDPAMLETA VKNIQAAMDK
TKTPVFGICL GHQLLARASG AKTEKMKFGN RGHNIPCTSM ISGKCHITSQ NHGFAVDSKS
LTADWRELFV NANDGSNEGI AHLSKPYFSV QFHPESTPGP RDTEYLFDVF ISTIENCAAD
PKLLNAPVSF PGGTIEENER LHPRVHPRKV LILGSGGLSI GQAGEFDYSG SQAIKALKEE
GIYTVLINPN IATIQTSKGL ADKVYFLPVN AEFVRKVIQY ERPDAIYVTF GGQTALQVGI
QLKDEFEELG VKVLGTPIDT IITTEDRELF ARSMDSIGEK CAKSASACNI DEAMSCVKDI
GFPVIVRAAY ALGGLGSGFA NNEAELLDLC NKAFAASPQV LIERSMKGWK EIEYEVVRDA
QDNCITVCNM ENFDPLGIHT GDSIVVAPSQ TLSDEDYNML RTTAVNVIRH LGVVGECNIQ
YALNPFSREY CIIEVNARLS RSSALASKAT GYPLAFIAAK LGLGIPLKDI ANSVTKSTCA
CFEPSLDYVV VKMPRWDLKK FTRVSTQLGS SMKSVGEVMS IGRSFEEAIQ KAIRAIDFHN
LGFNETKALM SIDDELQTPS DQRLFAIANA MHSGYTVEKI WELTKIDKWF LNKLKGLSDF
AKKMTNYTTS DISKSPDILL QAKRLGFSDR QLAKFWSSNE IAVRTLRQEA SIMPFVKQID
TVAAEFPAHT NYLYLTYNAT ESDVSFEDHG IMVLGSGVYR IGSSVEFDWC SVRAIRTLRR
DGFKTIMVNY NPETVSTDYD EADKLYFEVI SLESILDIYQ LENAAGVLGA MGGQTPNNIA
LPLHRAGIKI LGTSPEMIDN AENRYKFSRM LDTIGVDQPT WKELTSFEEA KKFCNAVSYP
VLVRPSYVLS GAAMNTVYSE QDLENYLAQA AEVSREHPVV ITKYIENAKE IEMDAVAKDG
VVIGHFISEH VENAGVHSGD ATLILPPQDL EPETIARIEE ATRKIGAALN VTGPFNIQFI
AKDNDIKVIE CNVRASRSFP FVSKVMGVDM IEMATKAITG RPFEAYPPTT IAPNCVGVKV
PQFSFSRLSG ADPVLGVEMA STGEVACFGV DKYEAYLKAL MSTGFKIPKA NILLSIGSYK
DKKEMLPAID KLARLGYKLF ATAGTADFLQ EHNIPVQYLE VLANEQEDQR SEFSLTQHLA
KNMIDLYINL PSNNKYRRPA NYMSKGYQTR RMAVDYQIPL VTNVKNAKIL VEAIARHFGL
EVGSRDFQTS HRTISLPGLI NVATFVPGIA TAGSKDLQAV TKASISAGFS MVRIMPVGVT
GSITDAITLK VAQQSSKQGG YCDYNFSVTA TSDNADQISH VTGEVGSLFI PFNHLSGNIS
KVAAVTAHFD KWPTHKPIVT DAKLTDLASI LLLASLHNRR IHVTSVSTKD DIKLIALSKA
KGLKVTCDVS IFSLYLSQND FPDCALLPTE ADQTALWAYL STIDVFSIGS LPYQLASSLG
KDADPSVGIA DALPLLLTSV TEGKLTVDDI KTRLYDNPKE IFELHEQVGT SVEVEIDRPY
AVHNTNGWSP FAGRTMRGSV QRVTFQDKTV CLDGELLPLP ALGKDMSTHG ALPMSPAIKP
QLQSLTHPDS PRDRRPSLFN TTRPSKLRST DGYLPNKSMS GFEDLGLPAP LHPVVSSKLQ
DLLSQPSSWK HHSVLSVSQY TRADLHHLFT VAQQMRLGVQ REGVLNILRG RVLCTLFYEP
STRTSASFDA AMQRLGGRTV AIATSHSSVQ KGETLQDTLR TLGCYGDAVV LRHPDEHSVD
IAKRYAPVPV INGGNGSKEH PTQAFLDLFT IREELGTVQG LTITFVGDLL YGRPVHSLIY
LLRDYGVQVQ LVSPKGLALP ADVRKFLVES GQLLCESEEL TPEILGRSDV LYCTRVQKER
FPSVEEYEKV KNSYRIDNRT LKSAKRDMCI LHPLPRNEEI APEVDTDQRA AYFRQMRYGL
YCRMALLALV MAP
//
