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MOC2B_DICDI
ID   MOC2B_DICDI             Reviewed;         158 AA.
AC   Q86HF4; Q55AG5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=MOCO1-B;
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=Molybdopterin synthase large subunit;
DE            Short=MPT synthase large subunit;
GN   Name=mocs2l; Synonyms=moco1l; ORFNames=DDB_G0271864;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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 mocs2s into precursor Z to generate a dithiolene
CC       group (By similarity). {ECO:0000250}.
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 (mocs2s) and 2 large
CC       (mocs2l) subunits. {ECO:0000250}.
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; AAFI02000007; EAL71511.1; -; Genomic_DNA.
DR   RefSeq; XP_645446.1; XM_640354.1.
DR   AlphaFoldDB; Q86HF4; -.
DR   SMR; Q86HF4; -.
DR   STRING; 44689.DDB0267170; -.
DR   PaxDb; Q86HF4; -.
DR   EnsemblProtists; EAL71511; EAL71511; DDB_G0271864.
DR   GeneID; 8618186; -.
DR   KEGG; ddi:DDB_G0271864; -.
DR   dictyBase; DDB_G0271864; mocs2l.
DR   eggNOG; KOG3307; Eukaryota.
DR   HOGENOM; CLU_089568_0_1_1; -.
DR   InParanoid; Q86HF4; -.
DR   OMA; WPLQRVS; -.
DR   PhylomeDB; Q86HF4; -.
DR   UniPathway; UPA00344; -.
DR   PRO; PR:Q86HF4; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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; ISS:UniProtKB.
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..158
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000331261"
FT   BINDING         107..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         130..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ   SEQUENCE   158 AA;  18017 MW;  A70838E19EEE41E4 CRC64;
     MSKESRIFIE ISENIIDLNY WYKIVSDDSS GATSSFLGTT RNEFKGKSVE RLEYETYEPM
     AIKEIEKICK TILNGFENDI KKIGIVHRIG NVPVGESSIL IVISSGHRKS SLEAVHYAID
     TIKSTVPIWK KEFYTDGSEN QWKGNCESCH FNNNNHPH
 
 
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