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MOAE_HELPJ
ID   MOAE_HELPJ              Reviewed;         145 AA.
AC   Q9ZL44;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=jhp_0736;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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}.
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DR   EMBL; AE001439; AAD06322.1; -; Genomic_DNA.
DR   PIR; G71893; G71893.
DR   RefSeq; WP_000913141.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZL44; -.
DR   SMR; Q9ZL44; -.
DR   STRING; 85963.jhp_0736; -.
DR   EnsemblBacteria; AAD06322; AAD06322; jhp_0736.
DR   KEGG; hpj:jhp_0736; -.
DR   eggNOG; COG0314; Bacteria.
DR   OMA; KWHHKAK; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000804; Chromosome.
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   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; Transferase.
FT   CHAIN           1..145
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000163085"
FT   BINDING         36..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   145 AA;  16683 MW;  0486C97C2C4E717D CRC64;
     MLKIVQGALD TDKLLKDYQE EACTKNFGAF CVFVGIVREE GNVQGLSFDI YEALLKTWFE
     KWRHQPKDLG VVLKMAHSVG DVLIRHSSFL CVLMGANTKN ALKLYEYFFK NFKRNAPIWK
     CYLSDNERIY AKKKDHLLKG SGLLA
 
 
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