ID   MOAE_SYNE7              Reviewed;         165 AA.
AC   Q56210; Q31NQ6;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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=Synpcc7942_1283;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9495759; DOI=10.1128/jb.180.5.1200-1206.1998;
RA   Rubio L.M., Flores E., Herrero A.;
RT   "The narA locus of Synechococcus sp. strain PCC 7942 consists of a cluster
RT   of molybdopterin biosynthesis genes.";
RL   J. Bacteriol. 180:1200-1206(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-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; X99625; CAA67947.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57313.1; -; Genomic_DNA.
DR   RefSeq; WP_011377957.1; NC_007604.1.
DR   AlphaFoldDB; Q56210; -.
DR   SMR; Q56210; -.
DR   STRING; 1140.Synpcc7942_1283; -.
DR   PRIDE; Q56210; -.
DR   EnsemblBacteria; ABB57313; ABB57313; Synpcc7942_1283.
DR   KEGG; syf:Synpcc7942_1283; -.
DR   eggNOG; COG0314; Bacteria.
DR   HOGENOM; CLU_089568_1_2_3; -.
DR   OMA; WPLQRVS; -.
DR   OrthoDB; 1877633at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1283-MON; -.
DR   UniPathway; UPA00344; -.
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; Transferase.
FT   CHAIN           1..165
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000163106"
FT   BINDING         42..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132..134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   165 AA;  18712 MW;  AC016984E1D587FB CRC64;
     MPDLLTCDRH QIELSLAPIP LSAAAEFCHD DRYGAFASFV GWVRRVNVGR LVTGITYQSF
     QPLCRTVLTE ICQEAEQVFG QELRIYVQHR LGETRVGDPT VLIGVGAIHR DEACEACRYV
     IEELKHRAPI WKLEHYEDGD SGWVPGNCLC QERRSRDRRG STGPE