MOC2A_AEDAE
ID MOC2A_AEDAE Reviewed; 98 AA.
AC Q1DGL5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Molybdopterin synthase sulfur carrier subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 small subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE Short=MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Sulfur carrier protein MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
GN Name=Mocs2-1 {ECO:0000255|HAMAP-Rule:MF_03051}; ORFNames=AAEL007643;
GN and
GN Name=Mocs2-1 {ECO:0000255|HAMAP-Rule:MF_03051}; ORFNames=AAEL015583;
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: Acts as a sulfur carrier required for molybdopterin
CC biosynthesis. Component of the molybdopterin synthase complex that
CC catalyzes the conversion of precursor Z into molybdopterin by mediating
CC the incorporation of 2 sulfur atoms into precursor Z to generate a
CC dithiolene group. In the complex, serves as sulfur donor by being
CC thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction
CC with MOCS2B, the sulfur is then transferred to precursor Z to form
CC molybdopterin. {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then
CC thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the large subunit (MOCS2B).
CC -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
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DR EMBL; CH901307; EAT32295.1; -; Genomic_DNA.
DR EMBL; CH477455; EAT40642.1; -; Genomic_DNA.
DR RefSeq; XP_001647627.1; XM_001647577.1.
DR RefSeq; XP_001658544.1; XM_001658494.1.
DR AlphaFoldDB; Q1DGL5; -.
DR SMR; Q1DGL5; -.
DR STRING; 7159.AAEL007643-PA; -.
DR eggNOG; KOG3474; Eukaryota.
DR HOGENOM; CLU_114601_4_3_1; -.
DR InParanoid; Q1DGL5; -.
DR OMA; LGTICER; -.
DR PhylomeDB; Q1DGL5; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_03051; MOCS2A; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR044672; MOCS2A.
DR InterPro; IPR028887; MOCS2A_euk.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR PANTHER; PTHR33359; PTHR33359; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..98
FT /note="Molybdopterin synthase sulfur carrier subunit"
FT /id="PRO_0000369308"
FT MOD_RES 98
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
FT MOD_RES 98
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
SQ SEQUENCE 98 AA; 10437 MW; 74DE5B718FC0C47A CRC64;
MSQGHRSEEV VRVNLLFFAK SRELVGTSSL DNFPLATSGG HLSGSAVLGT ICERFPELVA
IRDSVIIAHN EQYCEDLTEP ISLADGDEIA VIPPIAGG
