MOAE_STAAN
ID MOAE_STAAN Reviewed; 148 AA.
AC P65401; Q99S01;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=SA2066;
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 MOAD WITH OR WITHOUT
RP PRECURSOR Z, CATALYTIC ACTIVITY, AND REACTION 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: Converts molybdopterin precursor Z to 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.
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 Evidence={ECO:0000269|PubMed:18092812};
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; BA000018; BAB43363.1; -; Genomic_DNA.
DR PIR; B90025; B90025.
DR RefSeq; WP_000808495.1; NC_002745.2.
DR PDB; 2Q5W; X-ray; 2.00 A; E=1-148.
DR PDB; 2QIE; X-ray; 2.50 A; A/E/H/K=1-148.
DR PDBsum; 2Q5W; -.
DR PDBsum; 2QIE; -.
DR AlphaFoldDB; P65401; -.
DR SMR; P65401; -.
DR EnsemblBacteria; BAB43363; BAB43363; BAB43363.
DR KEGG; sau:SA2066; -.
DR HOGENOM; CLU_089568_1_2_9; -.
DR OMA; WPLQRVS; -.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P65401; -.
DR Proteomes; UP000000751; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Molybdenum cofactor biosynthesis; Transferase.
FT CHAIN 1..148
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163099"
FT BINDING 34..36
FT /ligand="substrate"
FT BINDING 44
FT /ligand="substrate"
FT BINDING 100..101
FT /ligand="substrate"
FT BINDING 116
FT /ligand="substrate"
FT BINDING 123..125
FT /ligand="substrate"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2Q5W"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2Q5W"
FT HELIX 53..70
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:2Q5W"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:2Q5W"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:2Q5W"
SQ SEQUENCE 148 AA; 17351 MW; B4293AEE3AD0C030 CRC64;
MKQFEIVIEP IQTEQYREFT INEYQGAVVV FTGHVREWTK GVKTEYLEYE AYIPMAEKKL
AQIGDEINEK WPGTITSIVH RIGPLQISDI AVLIAVSSPH RKDAYRANEY AIERIKEIVP
IWKKEIWEDG SKWQGHQKGN YEEAKREE
