MOAE_YERPE
ID MOAE_YERPE Reviewed; 151 AA.
AC Q8ZGW2; Q0WHN7;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Molybdopterin synthase catalytic subunit;
DE EC=2.8.1.12;
DE AltName: Full=MPT synthase subunit 2;
DE AltName: Full=Molybdenum cofactor biosynthesis protein E;
DE AltName: Full=Molybdopterin-converting factor large subunit;
DE AltName: Full=Molybdopterin-converting factor subunit 2;
GN Name=moaE; OrderedLocusNames=YPO1162, y3019, YP_0997;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Converts molybdopterin precursor Z into molybdopterin. This
CC requires the incorporation of two sulfur atoms into precursor Z to
CC generate a dithiolene group. The sulfur is provided by MoaD (By
CC 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;
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also
CC stable as homodimer. The enzyme changes between these two forms during
CC catalysis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MoaE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM86570.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS61248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL19826.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86570.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS61248.1; ALT_INIT; Genomic_DNA.
DR PIR; AH0142; AH0142.
DR RefSeq; YP_002346201.1; NC_003143.1.
DR AlphaFoldDB; Q8ZGW2; -.
DR SMR; Q8ZGW2; -.
DR STRING; 214092.YPO1162; -.
DR PaxDb; Q8ZGW2; -.
DR DNASU; 1147966; -.
DR EnsemblBacteria; AAM86570; AAM86570; y3019.
DR EnsemblBacteria; AAS61248; AAS61248; YP_0997.
DR KEGG; ype:YPO1162; -.
DR KEGG; ypk:y3019; -.
DR KEGG; ypm:YP_0997; -.
DR PATRIC; fig|214092.21.peg.1459; -.
DR eggNOG; COG0314; Bacteria.
DR HOGENOM; CLU_089568_2_1_6; -.
DR OMA; WPLQRVS; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..151
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163108"
FT BINDING 38..40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104..105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127..129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 151 AA; 17062 MW; C97CC2C4D09FD714 CRC64;
MMENTRIRVG AEAFSVGDEY TWLSQCDEDG AVVTFTGKVR NHNLGASVSA LTLEHYPGMT
EKALTEIIAD ARSRWSLQRV SVIHRVGPLF PGDEIVFVGV TSAHRSMAFE AAEFIMDYLK
TRAPFWKREA TVEGERWVES RDSDHIAAKR W
