ID A0A0D2CY44_9EURO Unreviewed; 934 AA.
AC A0A0D2CY44;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=GTP 3',8-cyclase {ECO:0000256|ARBA:ARBA00012167};
DE EC=4.1.99.22 {ECO:0000256|ARBA:ARBA00012167};
GN ORFNames=PV04_02420 {ECO:0000313|EMBL:KIW70116.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW70116.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW70116.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW70116.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-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}.
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DR EMBL; KN846957; KIW70116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2CY44; -.
DR STRING; 5601.A0A0D2CY44; -.
DR HOGENOM; CLU_009273_7_1_1; -.
DR OrthoDB; 9838at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000054266; 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; 1.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
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};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 96..315
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 17..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 103500 MW; 1908DFE4682753B0 CRC64;
MAEAGFRQLI AALLRQTRPQ SFRHSKPPRY PQRQLSTAAD APLRLPEPEL PQWQAHKVES
RPRPESDQVS EVKRPRLDKL RGEKEPRQFS SFLTDNYSRQ HNYLRISITE RCNLRCLYCM
PEEGVQLSPP AHLLTTPEIV YLAELFVGQG VDKIRLTGGE PTVRKDIVDL MHQIGKLRSN
GLRELCITTN GISLYRKLDS MVESGLTGIN LSLDTLDPHQ FAIMTRRNGH EAVMKSINRI
LEMNKLGAGV KLKINCVVMR GLNEREILPF VELGRNQEVE VRFIEYMPFD GNKWSEKKMM
SFGEMLALIR QKYPQVEKVR DHKNDTSKTY QVPGFAGRIG FITSMTHNFC GTCNRLRITS
DGNLKVCLFG NSEVSLRDIL RESNDGKPID AEAMEAIRQL EMDRRQQLSG STGALGVSEK
EAKLLNVIGM AVKRKEEKHA GIGDLENMKN RPMILIDDAP AAQRPPPSSY NTALPRHVSP
ISTFRQPLIP THLLHRSVSP PSWSQTRCFS SLFPVLPAGF RKFSNASSLT RSRLRYDAFR
YVHGQPTHRH VPTILPEDIP ASSGRTSEED RERSSSGASL AADIVIKSTA FREYMMSNIA
DRRKRKIARA RARRHSSTYG GGSNDAASTC PPLRSSTSPG KSSNSAPVAA EDEGQRSASL
SGFAVTNGTA TSADEVTTLT HLTADGEAHM VSIAQKKPTA RSATATSLLL FSHDGTYNVL
FASRLQKGDA LAVARIAGIQ AAKKTSDLIP LAHPGLDITG VTVRLEPFMG DNVPYPLSEA
FRIEGKKPHV AADVDTLHGG VLVTATVACE GKTGVEMEAI TAASVAGLTM YDMLKGVDKC
MVLTSTRVTA KSGGKSGDWE WDHQLHQRIV HHNPKPASEK TLEHQHSPSK QGKNQTLVQE
KARTAPVTAE DMRIQRLKRW NEHHDANQIH VPAG
//
