MOC2B_NEUCR
ID MOC2B_NEUCR Reviewed; 206 AA.
AC Q7SEW2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
DE AltName: Full=Nitrate nonutilizer protein 8;
GN Name=nit-8; ORFNames=7C14.140, NCU03170;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP GENE NAME.
RX PubMed=6449399; DOI=10.1093/genetics/95.3.649;
RA Tomsett A.B., Garrett R.H.;
RT "The isolation and characterization of mutants defective in nitrate
RT assimilation in Neurospora crassa.";
RL Genetics 95:649-660(1980).
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; BX842636; CAE76538.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA35340.1; -; Genomic_DNA.
DR RefSeq; XP_964576.1; XM_959483.2.
DR AlphaFoldDB; Q7SEW2; -.
DR SMR; Q7SEW2; -.
DR STRING; 5141.EFNCRP00000002859; -.
DR EnsemblFungi; EAA35340; EAA35340; NCU03170.
DR GeneID; 3880716; -.
DR KEGG; ncr:NCU03170; -.
DR VEuPathDB; FungiDB:NCU03170; -.
DR HOGENOM; CLU_089568_3_0_1; -.
DR InParanoid; Q7SEW2; -.
DR OMA; GEICLFV; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..206
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369358"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 154..156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ SEQUENCE 206 AA; 22293 MW; 920D293A6F8373A9 CRC64;
MATQQPTQTD NSAQAQPPQT NPAKPTEISE PGIYVALTHD HLNYQSVIDR VRSPEAGAIV
VFAGTTRNNF NSLPVQHLSY TSYAPLALRT MLTICRSILT KHGLKGIAMV HRLGVVPIGE
ESILIAVSSP HRQAAWRAGE EALEECKAKV EVWKREEFGG EGGGVWRANR DGAVGVKVDE
PRIGKGEVDE KEDEGDSGNG GNDRKS
