ID A0A0G2EDW0_9PEZI Unreviewed; 1252 AA.
AC A0A0G2EDW0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=GTP 3',8-cyclase {ECO:0000256|ARBA:ARBA00012167};
DE EC=4.1.99.22 {ECO:0000256|ARBA:ARBA00012167};
GN ORFNames=UCDDS831_g04793 {ECO:0000313|EMBL:KKY20451.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY20451.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY20451.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY20451.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY20451.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY20451.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-
CC methionine; Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:131766; EC=4.1.99.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000034};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoaC family.
CC {ECO:0000256|ARBA:ARBA00008484}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. MoaA family. {ECO:0000256|ARBA:ARBA00009862}.
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:KKY20451.1}.
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DR EMBL; LAQI01000100; KKY20451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EDW0; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000034182; Unassembled WGS sequence.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21117; Twitch_MoaA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR010505; MoaA_twitch.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02666; moaA; 1.
DR PANTHER; PTHR22960:SF0; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN 1; 1.
DR PANTHER; PTHR22960; MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A; 1.
DR Pfam; PF01967; MoaC; 2.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDG01216; thioether_bond_formation_requi; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 2.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 91..319
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 560..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1189
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 141540 MW; 666C302F552F1AD5 CRC64;
MAGHIVRARA HALRTQSLAA ARRPHILGGK LVPPATSYRT IAPRRITTAA VAPQPSLEVP
AAQVEFPPPP QQDRRDAIKQ AKPFSEFLTD TFNRQHDYLR ISITERCNLR CLYCMPEEGV
PLSPPDHLLT SPEIFYISSL FVSQGVNKIR LTGGEPTVRR DIVPLMRSIG SLRSKGLREL
AITTNGISLH RKLDSMVESG LTGINLSLDT LDPFQFTLMT RRKGFDAVMR SVERVLEMKR
LGAPVKLKIN CVVMRGLNDR EIVPFVELGR EKDVEVRFIE YMPFDGNRWN QKKMMSYQEM
LDVIRAKYPG ARPVQGHKND TSKTWEIPGF VGKFGFITSM THNFCGTCNR LRITSDGNLK
VCLFGNTEVS LRDIMRKDND GKPIDEAAFE AIKEVEMNRH QGLLGEGSSP AWSERERELL
EVIGAAVKRK KEKHAGMGEL ENMKNRPMIL IEDDDTYNEQ EEQRDRPIKL THVNQNGTAH
MVSVWNKGNT RRTAFAVSSI RFSRPEPIML IKKNAIQKGD VLSTARIAGI MAAKQTANII
PLCHNINISH AEVEAGLIEP PQSSSDAATT TSSQDASSDE ANNNTTTEDA FYADDPPDAA
QGFSLRRPGS RARLIATSHL THGDARAVPA DVDPAAAYPH GGVLLTARVE TVGPTGVEMD
ALHAASAAAL TVFDMCKAVD RAMSVQNSRV VLKTGGRSGD WVDEGWLYAK AGVVLPPLPT
TAGSGGEQRF QMNRKPASTL SLGETVQILR EQWKNANSTD AAGNGQGSTR LTASMIRKMS
AQDIFADDVN PRKTNHNVWA AEALKTEVEQ QQQHAEQNKK PKVKQKQPEM EQETPEVKQK
QPETEQAKPK TEQHEQILEQ EEMEDRDKEM EKSGDDPFEH IAIAAALPKR DAARGTGLTL
PDIQPTSKEA RSAQKSTISA PAPRGDHPLM PYEVRRMERD AVWDKRMERL AALDRLAHQA
RRSPKFSPHW ERARSWGRAA MRTVELAAAI GQHTSPCDVL QWEPPAGAVP ATRAGRQALR
LSWAAFRKDA TPMAWWVQER NFPHRIRERH FLKEEKAGLK RAMGRINYNE WTLLTGIAAK
RERRWAVQRE KESQERQAAA NARALLESDL SGDQWYDKLL EEAERDEEGE MERDEEGEME
RDEELEMERD EELEMERDEE LEMESDEEGE MEKDEEGKME SDEEGEMEKD EEGKVERNEE
DAREPMKIGL PIKEQWYDEV MEEEERRLLH RRMDKKWATR EKWEIKNRKK WE
//
