ID A0A2T9YKA2_9FUNG Unreviewed; 2363 AA.
AC A0A2T9YKA2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PVU92770.1};
GN ORFNames=BB559_003596 {ECO:0000313|EMBL:PVU92770.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU92770.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU92770.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU92770.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU92770.1}.
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DR EMBL; MBFT01000347; PVU92770.1; -; Genomic_DNA.
DR STRING; 61424.A0A2T9YKA2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000245699; 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; 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:UP000245699};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 622..814
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1140..1331
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1396..1565
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1879..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1890..1906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2363 AA; 260251 MW; E9DBD49094BC2E44 CRC64;
MVINVNEEVK HMQGIVSGRS SPVGRIQNPY QPCVAPVESF SLSEGVRPLE SLSKLPPNLL
TLVMEDGSMY LGYSFGSEKK SVSGELVFQT GMTGYPEALT DPSNKGYLLV LTFPLIGNYG
VPDDTKFDEL LKDRLEFFES SKIHVTGLII GNLSSEYSHY LAKTSLSEWL IKNEIPAMYG
VDTRAITKKI REQGAMIGKM LFQKSLVGPG EPTSDMGSEG WMKTLSNVEW NDINKENLVS
QVSTKVSHLY VPKPGTELKH PTENRTLRIV AVDLGLKNKQ LTFMVGMGLE VKLVPWDHDF
LKEDIIDGLF LSNGPGNPDA IPRETVVARA QKAIKLEKFP IFGICMGHQL LSIASGASLT
KMKYGNRGAN IPCTDLRTGR CYITSQNHGY AINANTYPDT CTELFINAND GTNEGMMYKN
LPYFSVQFHP ESTPGPSDTE FLFADFIDLI KRCAGKSSVR GIPVRGGDVQ ANIKNEFMLS
QSGALKKVGG RIVNGKIIRK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE EGIYTILINP
NIATIQTSKG LADKCYFLPV TPDCVRKVIQ YERPDGIYCT FGGQTALNIG VQLCDEFEQL
GVQVLGTQIS TIMKTEDREL FANALAEISE KCAESRTAIN VEEAIEAGNI IGYPVIVRAA
YALGGLGSGF ASNEEELRDL STKAFSSSPQ ILVERSMKGW KEVEFEVVRD SADNCIVVCN
MENFDPLGIH TGDSIVVAPC MTLSDSDVQM LRTTAIKVVR HLGVVGECNI QYALNPDSNE
YCIIEVNARL SRSSALASKA TGYPLAFVAA KLGLGIKLNS IRNSVTRVTT ACFEPKLSSA
MKSVGEVMAI GRTFEECLME AIRSVESAFT GFSSNEYTST DREDIDRELS QPTDKRLFAI
ANAFHLGYTV EQIWQLTRID RWFLCRLRSL VETEKKLAAT SSLGHIPTAL FRTAKQLGFS
DRGIAHITKG NEFQIRRDRR ALGLHPFVKQ IDTVAAEFPA VTNYLYLTYN ASTHDVDFND
RGVMVLGSGV YRIGSSVEFD WCAVRAIGTL RANNYKTIMV NYNPETVSTD YDEADRLYFS
NISLERVLDI YELEQSAGVV VAMGGQAPNN IALALHRQKV NILGTSPDYI DNAENRYKFS
RMLDQIGIDQ PAWRELTQLE DAHAFCKEVG FPVLVRPSYV LSGAAMNVVF TADDLRNYLE
QAATVSREYP VVISKFIEDA KEIDVDAVAV DGKMIVHFIS EHVENAGVHS GDATLVLPPQ
DLDPITVRKI EEATAAIGKA LHVTGPYNIQ FIAKNNEIKV IECNVRAARS FPFVSKAMNV
DLVELSIKAM LKIPISYKPS KTPPKYVAVK VPQFSFSRLL GADPILGVEM ASTGEVAAFG
PDKYSAYMKA LLATGFKIPN KNVLVSIGSY KEKVEMLDYI KKLVKLGFNI FATAGTEDFF
SENNVQVKFL DSSTSQKYNM HEHLANNLID LYINLPSKNS YRRPASFMSE GYKSRRMAID
CSIPLITNVK CAKMFIEALS RYPPKHWEIE NSDYITSHRT VIIPGLVDIA SNVILGGSID
RKIVKKNTSS ALYGGFTTLS ILSPNFDGQD KPVFQNLNQA LGPVASSCFA TDYVISVPST
ASVSELSQIN SGASVLYIQK SSEPKTSSSD YAAVSGIFRT WPTNLPIITD VYGTNLASTL
LLASLFDRSV HITNVSSSDD LMLIRLSKEK GLNVSCDVSV FSLFPLPPSS IQECKDDLEV
NRFNLWANMD SIDCFSVGRV PKKISSLLNE SEAIKLAYSL SLPLLLSAVS YGKISVKEIV
SKFSTNPRKI LGLSEQPDTF IEVQLDRTIP LVQAITPISD KALSAVTDTY GIEFHNSLHR
VVYFGTTVYL DGRIKSEGTA TRPARDLSKD IHTSSSGPSK KDVHALSNEV SGQKSNIDGD
FKVLPDLSPF AQISPSKSAT LSKPKSKKID VSGEPLLSVG VHSISGRRVS IDSSNRKKVN
NMDFNTGFDD ENATASGTDE GLDDGVSEYA ESNRVVKARP SKLMPISYNK SLHLTFLPSI
LERFGGNNPF YSQSIISVRQ LSKNHLYLLF AVAMEIRIIV EKHGMIPLLS GKVMASVFYE
PSSRTSASFQ AAMLRLGGQV FSINSESSSS TKGESLADTI RTFSSYADCI VLRHPDRGAA
RSVADLNDIP ILNAGDGTGE HPTQAMLDVF TIREELGTVN GLVITMVGDL KNGRTVHSLS
RVLALYNNIT INYIAPTEDM QMPEYIIDEI NQKADTRNIK QYKYGNLTDE ILANTDVLYV
TRIQKERFKS IEEYNEIVNK NFIVNNSTLN KCKKNMIVMH PLPRVNEISV DVDTDPRAAY
FRQMKYGMYV RMALLSLVLS SPY
//
