MOC2B_EMENI
ID MOC2B_EMENI Reviewed; 195 AA.
AC Q9Y8C1; C8VA81; Q5B3N9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=AN4841;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-74; ALA-108;
RP GLY-148; GLU-166 AND ARG-195.
RX PubMed=10383438; DOI=10.1074/jbc.274.27.19286;
RA Unkles S.E., Heck I.S., Appleyard M.V.C.L., Kinghorn J.R.;
RT "Eukaryotic molybdopterin synthase. Biochemical and molecular studies of
RT Aspergillus nidulans cnxG and cnxH mutants.";
RL J. Biol. Chem. 274:19286-19293(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AF138285; AAD39471.1; -; Genomic_DNA.
DR EMBL; AACD01000083; EAA60076.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF76656.1; -; Genomic_DNA.
DR RefSeq; XP_662445.1; XM_657353.1.
DR AlphaFoldDB; Q9Y8C1; -.
DR SMR; Q9Y8C1; -.
DR STRING; 162425.CADANIAP00005571; -.
DR EnsemblFungi; CBF76656; CBF76656; ANIA_04841.
DR EnsemblFungi; EAA60076; EAA60076; AN4841.2.
DR GeneID; 2872641; -.
DR KEGG; ani:AN4841.2; -.
DR VEuPathDB; FungiDB:AN4841; -.
DR eggNOG; KOG3307; Eukaryota.
DR HOGENOM; CLU_089568_3_1_1; -.
DR InParanoid; Q9Y8C1; -.
DR OMA; WPLQRVS; -.
DR OrthoDB; 1419096at2759; -.
DR BRENDA; 2.8.1.12; 517.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; 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 GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:AspGD.
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 1: Evidence at protein level;
KW Cytoplasm; Molybdenum cofactor biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..195
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369355"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 164..166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT MUTAGEN 74
FT /note="G->D: In cnxH89; impairs molybdopterin
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:10383438"
FT MUTAGEN 108
FT /note="A->T: In cnxH35/cnxH36; impairs molybdopterin
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:10383438"
FT MUTAGEN 148
FT /note="G->D: In cnxH604; impairs molybdopterin
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:10383438"
FT MUTAGEN 148
FT /note="G->GG: In cnxH255; impairs molybdopterin
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:10383438"
FT MUTAGEN 166
FT /note="E->K: In cnxH43; impairs molybdopterin
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:10383438"
FT MUTAGEN 195
FT /note="R->RCLESYGTRLDRMDIINTRMVAWTRKGNILIPL: In cnxH1;
FT impairs molybdopterin biosynthesis."
FT /evidence="ECO:0000269|PubMed:10383438"
SQ SEQUENCE 195 AA; 21611 MW; 3739F6505A7CD152 CRC64;
MSARPEPQPG SERNATEPLP SHLDPTTYPR TLTTTHGPTS IPLHLELTYH TLSPTTALQH
VSSPSSGANI LFLGTTRDTF DDRPVARLSY TSYPALALKS LHKISSEAVE KFGLNGVYIA
HRLGEVPVGE ASIVVAVGAG HRGEAWRGAE WVLEVVKERV EVWKREEFVD GGMEWRENRE
RDGFGKLKTK KEDSR
