ID   MOC2B_RAT               Reviewed;         200 AA.
AC   Q6AY59;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=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=Mocs2 {ECO:0000255|HAMAP-Rule:MF_03052};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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, cytosol {ECO:0000255|HAMAP-
CC       Rule:MF_03052}.
CC   -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC       also produces the small subunit (MOCS2A) from an overlapping reading
CC       frame.
CC   -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR   EMBL; BC079181; AAH79181.1; -; mRNA.
DR   RefSeq; NP_001007634.1; NM_001007633.2.
DR   RefSeq; NP_001155885.1; NM_001162413.1.
DR   RefSeq; XP_017446205.1; XM_017590716.1.
DR   AlphaFoldDB; Q6AY59; -.
DR   SMR; Q6AY59; -.
DR   STRING; 10116.ENSRNOP00000015781; -.
DR   PaxDb; Q6AY59; -.
DR   Ensembl; ENSRNOT00000082990; ENSRNOP00000073722; ENSRNOG00000056325.
DR   GeneID; 294753; -.
DR   KEGG; rno:294753; -.
DR   CTD; 4338; -.
DR   RGD; 1359477; Mocs2.
DR   eggNOG; KOG3307; Eukaryota.
DR   GeneTree; ENSGT00510000047669; -.
DR   HOGENOM; CLU_089568_0_1_1; -.
DR   InParanoid; Q6AY59; -.
DR   OMA; WPLQRVS; -.
DR   OrthoDB; 1419096at2759; -.
DR   PhylomeDB; Q6AY59; -.
DR   TreeFam; TF314334; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000056325; Expressed in quadriceps femoris and 20 other tissues.
DR   Genevisible; Q6AY59; RN.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0019008; C:molybdopterin synthase complex; ISO:RGD.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0030366; F:molybdopterin synthase activity; ISO:RGD.
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   2: Evidence at transcript level;
KW   Cytoplasm; Molybdenum cofactor biosynthesis; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..200
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000369327"
FT   REGION          16..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         154..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         177..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O96007"
SQ   SEQUENCE   200 AA;  22233 MW;  8CCEF5D50263F879 CRC64;
     MSSLEINNSC FSLETKLPSS HQSVEDSASE PSGYEAKDPP QDTLKDVDDV LEKPKDIIQF
     TAKKLSVGEV SQLVVSPLCG AVSLFVGTTR NNFEGKKVIS LEYEAYLPMA ENEIRKICND
     IRQKWPVRHI AVFHRLGLVP VSEASTVIAV SSAHRAASLE AVSYAIDSLK AKVPIWKKEI
     YEESTSSWKR NKECFWAADD