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MOAE_PSEAE
ID   MOAE_PSEAE              Reviewed;         150 AA.
AC   Q9HX97;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=PA3916;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG07303.1; -; Genomic_DNA.
DR   PIR; B83156; B83156.
DR   RefSeq; NP_252605.1; NC_002516.2.
DR   RefSeq; WP_003093025.1; NZ_QZGE01000001.1.
DR   AlphaFoldDB; Q9HX97; -.
DR   SMR; Q9HX97; -.
DR   STRING; 287.DR97_3950; -.
DR   PaxDb; Q9HX97; -.
DR   PRIDE; Q9HX97; -.
DR   EnsemblBacteria; AAG07303; AAG07303; PA3916.
DR   GeneID; 878985; -.
DR   KEGG; pae:PA3916; -.
DR   PATRIC; fig|208964.12.peg.4102; -.
DR   PseudoCAP; PA3916; -.
DR   HOGENOM; CLU_089568_2_1_6; -.
DR   InParanoid; Q9HX97; -.
DR   OMA; GEICLFV; -.
DR   PhylomeDB; Q9HX97; -.
DR   BioCyc; PAER208964:G1FZ6-3989-MON; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002438; 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..150
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000163090"
FT   BINDING         35..37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         101..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   150 AA;  16686 MW;  04479BDDFDFF5459 CRC64;
     MAIRVQQAAF DPGQELNALH AQNVGIGAVV GFVGYVRDFN DGREVGGMFL EHYPGMTEKA
     LGKIAAEAGQ RWPLLRLEIL HRIGRLEPGE PIVFVGCASA HRQAAFDACN FVMDYLKTRA
     PFWKKEDTAE GPRWVEGRCS DQAAAQRWEE
 
 
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