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MO2B2_AEDAE
ID   MO2B2_AEDAE             Reviewed;         155 AA.
AC   Q1DGL6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Molybdopterin synthase catalytic subunit 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_03052};
DE   AltName: Full=Molybdenum cofactor synthesis protein 2B 2 {ECO:0000255|HAMAP-Rule:MF_03052};
DE            Short=MOCS2B 2 {ECO:0000255|HAMAP-Rule:MF_03052};
GN   Name=Mocs2-2 {ECO:0000255|HAMAP-Rule:MF_03052}; ORFNames=AAEL015584;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
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   -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC       also produces the large subunit (MOCS2A).
CC   -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR   EMBL; CH901307; EAT32294.1; -; Genomic_DNA.
DR   RefSeq; XP_001647626.1; XM_001647576.1.
DR   AlphaFoldDB; Q1DGL6; -.
DR   SMR; Q1DGL6; -.
DR   STRING; 7159.AAEL015584-PA; -.
DR   eggNOG; KOG3307; Eukaryota.
DR   HOGENOM; CLU_089568_0_1_1; -.
DR   InParanoid; Q1DGL6; -.
DR   OMA; WPLQRVS; -.
DR   PhylomeDB; Q1DGL6; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000008820; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..155
FT                   /note="Molybdopterin synthase catalytic subunit 2"
FT                   /id="PRO_0000369330"
FT   BINDING         101..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         124..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ   SEQUENCE   155 AA;  17637 MW;  96820397906FCF4D CRC64;
     MNYLKLTFDK LEVGEINDLV AHESCGAISL FVGTTRDNFD GKTVVLLEYE AYEAMALKTM
     NQICEELRAR WPDIKHIGIH HRLGTVPVKE ASVVIAVSSP HRKSSLEAVH FAIDELKKSV
     PVWKKEQYAE GEGCSEWKEN KECSWSKSHR DNHIL
 
 
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