MOC2B_DROME
ID MOC2B_DROME Reviewed; 367 AA.
AC Q9VBX2; Q961W4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
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=Mocs2B {ECO:0000312|FlyBase:FBgn0039280};
GN Synonyms=Mocs2 {ECO:0000255|HAMAP-Rule:MF_03052};
GN ORFNames=CG10238 {ECO:0000312|FlyBase:FBgn0039280};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP IDENTIFICATION.
RX PubMed=18237443; DOI=10.1186/1471-2164-9-61;
RA Hayden C.A., Bosco G.;
RT "Comparative genomic analysis of novel conserved peptide upstream open
RT reading frames in Drosophila melanogaster and other dipteran species.";
RL BMC Genomics 9:61-61(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATAC COMPLEX,
RP AND SUBCELLULAR LOCATION.
RX PubMed=18327268; DOI=10.1038/nsmb.1397;
RA Suganuma T., Gutierrez J.L., Li B., Florens L., Swanson S.K.,
RA Washburn M.P., Abmayr S.M., Workman J.L.;
RT "ATAC is a double histone acetyltransferase complex that stimulates
RT nucleosome sliding.";
RL Nat. Struct. Mol. Biol. 15:364-372(2008).
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 (By similarity). Component of the Ada2a-containing
CC (ATAC) complex composed of at least Ada2a, Atac1, Hcf, Ada3, Gcn5,
CC Mocs2B, Charac-14, Atac3, Atac2, NC2beta and wds (PubMed:18327268).
CC {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:18327268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03052}.
CC Nucleus {ECO:0000269|PubMed:18327268}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the small subunit (Mocs2A).
CC -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR EMBL; AE014297; AAF56405.2; -; Genomic_DNA.
DR EMBL; AY047520; AAK77252.1; -; mRNA.
DR RefSeq; NP_651340.1; NM_143083.3.
DR AlphaFoldDB; Q9VBX2; -.
DR SMR; Q9VBX2; -.
DR BioGRID; 67937; 34.
DR IntAct; Q9VBX2; 21.
DR STRING; 7227.FBpp0084157; -.
DR PaxDb; Q9VBX2; -.
DR PRIDE; Q9VBX2; -.
DR DNASU; 43017; -.
DR EnsemblMetazoa; FBtr0084782; FBpp0084157; FBgn0039280.
DR GeneID; 43017; -.
DR KEGG; dme:Dmel_CG10238; -.
DR UCSC; CG10238-RA; d. melanogaster.
DR CTD; 43017; -.
DR FlyBase; FBgn0039280; Mocs2B.
DR VEuPathDB; VectorBase:FBgn0039280; -.
DR eggNOG; KOG3307; Eukaryota.
DR GeneTree; ENSGT00510000047669; -.
DR HOGENOM; CLU_045449_0_0_1; -.
DR InParanoid; Q9VBX2; -.
DR OMA; GIAIYHR; -.
DR PhylomeDB; Q9VBX2; -.
DR SignaLink; Q9VBX2; -.
DR UniPathway; UPA00344; -.
DR BioGRID-ORCS; 43017; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43017; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039280; Expressed in midgut and 12 other tissues.
DR Genevisible; Q9VBX2; DM.
DR GO; GO:0140672; C:ATAC complex; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019008; C:molybdopterin synthase complex; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0030366; F:molybdopterin synthase activity; ISS:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:FlyBase.
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 1: Evidence at protein level;
KW Cytoplasm; Molybdenum cofactor biosynthesis; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..367
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000369336"
FT REGION 325..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 367 AA; 41891 MW; 82C9354DDD24D3B9 CRC64;
MDHVKLVNDP IDIAHIHQLL ADEGCGASSV FVGTTRDNFQ GKKVLSLAYE AYDSMALKEM
NKICSDLRSK WLDLKHIVIY HRLGTVPVCE ASVVIAASSP HRSEALESVS FAIDQLKTRV
PIWKKEIYDG DNDSEWKENK ESIRPKKSKS GFNYAACPCK VEESHDVPRT LVQIRVNDAE
LTKRLECFVN RKRDEINSQN VIDFKSSFVS SDQNLSDSCA RTQSTIIKQE QSNCHLKVRR
VNNRCGPQQM EMRPNYELEL NKLMGSRDGQ TDPTKEMRKS LPNSRLQAIE SYMGLTTDNE
ENIFSRIKRV ENRLLQLESI SPEYRHFTKR EPSSMEAAPP KKSRKKSYSA QELSAFIQKI
KDGSELS
