ID   MOAD_STAAN              Reviewed;          77 AA.
AC   Q7A441;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=SA2065;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MOAE, AND REACTION
RP   MECHANISM.
RX   PubMed=18092812; DOI=10.1021/bi701734g;
RA   Daniels J.N., Wuebbens M.M., Rajagopalan K.V., Schindelin H.;
RT   "Crystal structure of a molybdopterin synthase-precursor Z complex: insight
RT   into its sulfur transfer mechanism and its role in molybdenum cofactor
RT   deficiency.";
RL   Biochemistry 47:615-626(2008).
RN   [3]
RP   ERRATUM OF PUBMED:18092812.
RA   Daniels J.N., Wuebbens M.M., Rajagopalan K.V., Schindelin H.;
RL   Biochemistry 47:3315-3315(2008).
CC   -!- FUNCTION: Involved in sulfur transfer in the conversion of
CC       molybdopterin precursor Z to molybdopterin.
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   -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC       adenylated (-COAMP) by MoeB, then thiocarboxylated (-COSH) by IscS.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MoaD family. {ECO:0000305}.
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DR   EMBL; BA000018; BAB43362.1; -; Genomic_DNA.
DR   RefSeq; WP_000866971.1; NC_002745.2.
DR   PDB; 2Q5W; X-ray; 2.00 A; D=1-77.
DR   PDB; 2QIE; X-ray; 2.50 A; B/D/G/J=1-77.
DR   PDBsum; 2Q5W; -.
DR   PDBsum; 2QIE; -.
DR   AlphaFoldDB; Q7A441; -.
DR   SMR; Q7A441; -.
DR   EnsemblBacteria; BAB43362; BAB43362; BAB43362.
DR   KEGG; sau:SA2065; -.
DR   HOGENOM; CLU_114601_4_1_9; -.
DR   OMA; SEMDINC; -.
DR   UniPathway; UPA00344; -.
DR   EvolutionaryTrace; Q7A441; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR044672; MOCS2A.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR003749; ThiS/MoaD-like.
DR   PANTHER; PTHR33359; PTHR33359; 1.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; SSF54285; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN           1..77
FT                   /note="Molybdopterin synthase sulfur carrier subunit"
FT                   /id="PRO_0000392067"
FT   MOD_RES         77
FT                   /note="1-thioglycine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         77
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000250"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   HELIX           7..13
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   HELIX           28..38
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:2Q5W"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:2Q5W"
SQ   SEQUENCE   77 AA;  8871 MW;  018E805A2FEE3B31 CRC64;
     MKVLYFAEIK DILQKAQEDI VLEQALTVQQ FEDLLFERYP QINNKKFQVA VNEEFVQKSD
     FIQPNDTVAL IPPVSGG