MOC2B_PHANO
ID MOC2B_PHANO Reviewed; 188 AA.
AC Q0V713;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE EC=2.8.1.12 {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein H {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 large subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2B {ECO:0000255|HAMAP-Rule:MF_03052};
DE Short=MOCS2B {ECO:0000255|HAMAP-Rule:MF_03052};
GN Name=cnxH {ECO:0000255|HAMAP-Rule:MF_03052}; ORFNames=SNOG_00201;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a
CC complex that catalyzes the conversion of precursor Z into
CC molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms
CC from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene
CC group. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly +
CC 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160,
CC Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03052};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR EMBL; CH445325; EAT91696.2; -; Genomic_DNA.
DR RefSeq; XP_001790894.1; XM_001790842.1.
DR AlphaFoldDB; Q0V713; -.
DR SMR; Q0V713; -.
DR STRING; 13684.SNOT_00201; -.
DR EnsemblFungi; SNOT_00201; SNOT_00201; SNOG_00201.
DR GeneID; 5968456; -.
DR KEGG; pno:SNOG_00201; -.
DR eggNOG; KOG3307; Eukaryota.
DR HOGENOM; CLU_089568_3_1_1; -.
DR InParanoid; Q0V713; -.
DR OrthoDB; 1419096at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR HAMAP; MF_03052; MOC2B; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR028888; MOCS2B_euk.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Molybdenum cofactor biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..188
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369359"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 146..148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ SEQUENCE 188 AA; 20237 MW; 4C2C1A37E74533F4 CRC64;
MSTSETSSYT PDIPSEPVTK TTDTIHIELT PNDLDSLAAT RFVRSPSAGA TVLFIGTTRD
SFNDKAVSSL SYTSYAPLAI STLYKIASNI LTKHACTKIA IIHKLGECPI GEESIVIAVS
APHRKAAWLA GEEALEETKD KAEIWKLERF EGGEGVWRAN RDGKVGERVD GGIAGLLGRI
EVFADTNV
