ID   MOC2B_ASPFC             Reviewed;         188 AA.
AC   B0XYQ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=AFUB_041710;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499596; EDP53000.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XYQ4; -.
DR   SMR; B0XYQ4; -.
DR   EnsemblFungi; EDP53000; EDP53000; AFUB_041710.
DR   VEuPathDB; FungiDB:AFUB_041710; -.
DR   HOGENOM; CLU_089568_3_1_1; -.
DR   PhylomeDB; B0XYQ4; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
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; Transferase.
FT   CHAIN           1..188
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000369350"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134..135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         157..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ   SEQUENCE   188 AA;  20615 MW;  BE04E6BE2796A23F CRC64;
     MATQPPQDQT STTPSLPPHL DPTTYPRILT SATHNIHLEL TYSTLNPTVA LEHTSSPAAG
     ANVLFLGTTR DTFEGRAVSQ LSYTSYPPLA LKSLMSIATR AVEKFDLKGV YIAHRLGVVP
     ISEASIVVAV SAGHRGMAWK AAEEVLEEVK EKVEIWKREE FVDGGMEWRE NRERDAEGRI
     LSSTEGGK