ID   MOAD_SYNE7              Reviewed;          90 AA.
AC   Q56209; Q31NQ5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Molybdopterin synthase sulfur carrier subunit;
DE   AltName: Full=MPT synthase subunit 1;
DE   AltName: Full=Molybdenum cofactor biosynthesis protein D;
DE   AltName: Full=Molybdopterin-converting factor small subunit;
DE   AltName: Full=Molybdopterin-converting factor subunit 1;
DE   AltName: Full=Sulfur carrier protein MoaD;
GN   Name=moaD; OrderedLocusNames=Synpcc7942_1284;
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: Involved in sulfur transfer in the conversion of
CC       molybdopterin precursor Z to molybdopterin. {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Forms a
CC       stable heterotetrameric complex of 2 MoaD and 2 MoeB during adenylation
CC       of MoaD by MoeB. During catalysis MoaD shuttles between the two
CC       heterotetrameric complexes (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MoaD family. {ECO:0000305}.
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DR   EMBL; X99625; CAA67946.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57314.1; -; Genomic_DNA.
DR   RefSeq; WP_011377958.1; NC_007604.1.
DR   AlphaFoldDB; Q56209; -.
DR   SMR; Q56209; -.
DR   STRING; 1140.Synpcc7942_1284; -.
DR   PRIDE; Q56209; -.
DR   EnsemblBacteria; ABB57314; ABB57314; Synpcc7942_1284.
DR   KEGG; syf:Synpcc7942_1284; -.
DR   HOGENOM; CLU_2439693_0_0_3; -.
DR   OMA; RACDLMP; -.
DR   BioCyc; SYNEL:SYNPCC7942_1284-MON; -.
DR   UniPathway; UPA00344; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Phosphoprotein.
FT   CHAIN           1..90
FT                   /note="Molybdopterin synthase sulfur carrier subunit"
FT                   /id="PRO_0000209133"
FT   MOD_RES         90
FT                   /note="1-thioglycine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         90
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   90 AA;  9244 MW;  146128988EC0C76E CRC64;
     MTTTITLICF GGLAALSPEG QPMPLELDLP ATAADLKVAI ARACDLMPDS ALAQLLQKSA
     IGSETRIYID SDLIPASLSH LALLPPVSGG