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MOAE_CERS4
ID   MOAE_CERS4              Reviewed;         146 AA.
AC   Q53091; Q3IYX9;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=RHOS4_26870; ORFNames=RSP_1071;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8576035; DOI=10.1128/jb.178.4.1030-1038.1996;
RA   Dryden S.C., Dowhan W.;
RT   "Isolation and expression of the Rhodobacter sphaeroides gene (pgsA)
RT   encoding phosphatidylglycerophosphate synthase.";
RL   J. Bacteriol. 178:1030-1038(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; U29587; AAC44004.1; -; Genomic_DNA.
DR   EMBL; CP000143; ABA80255.1; -; Genomic_DNA.
DR   RefSeq; WP_002721436.1; NZ_CP030271.1.
DR   RefSeq; YP_354156.1; NC_007493.2.
DR   AlphaFoldDB; Q53091; -.
DR   SMR; Q53091; -.
DR   STRING; 272943.RSP_1071; -.
DR   EnsemblBacteria; ABA80255; ABA80255; RSP_1071.
DR   KEGG; rsp:RSP_1071; -.
DR   PATRIC; fig|272943.9.peg.3045; -.
DR   eggNOG; COG0314; Bacteria.
DR   OMA; WPLQRVS; -.
DR   PhylomeDB; Q53091; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002703; Chromosome 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..146
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000163094"
FT   BINDING         35..37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         99..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   146 AA;  15779 MW;  B2DDAE3FB8DD22B0 CRC64;
     MRVLVQAEPF EFGAEAQTFA DGAAGAGAIV TFTGLVRDLS GALEAMEIEH YPGMTERAIA
     AIAEEARQRW HLIDALVIHR HGRLGPSEPI MMVATAAAHR AEAFAAAEFL MDYLKSRAPF
     WKKEVTAGGA DWVAAKEADE AALGRW
 
 
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