MOAE_HELPY
ID MOAE_HELPY Reviewed; 145 AA.
AC P56422;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=HP_0800;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 -!- INTERACTION:
CC P56422; O25482: HP_0801; NbExp=3; IntAct=EBI-7674385, EBI-7674271;
CC -!- SIMILARITY: Belongs to the MoaE family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07850.1; -; Genomic_DNA.
DR PIR; H64619; H64619.
DR RefSeq; NP_207593.1; NC_000915.1.
DR RefSeq; WP_000912676.1; NC_018939.1.
DR PDB; 3RPF; X-ray; 1.90 A; A/B=2-145.
DR PDBsum; 3RPF; -.
DR AlphaFoldDB; P56422; -.
DR SMR; P56422; -.
DR DIP; DIP-3522N; -.
DR IntAct; P56422; 9.
DR MINT; P56422; -.
DR STRING; 85962.C694_04100; -.
DR PaxDb; P56422; -.
DR DNASU; 898921; -.
DR EnsemblBacteria; AAD07850; AAD07850; HP_0800.
DR KEGG; hpy:HP_0800; -.
DR PATRIC; fig|85962.47.peg.852; -.
DR eggNOG; COG0314; Bacteria.
DR OMA; KWHHKAK; -.
DR PhylomeDB; P56422; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..145
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163086"
FT BINDING 36..38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3RPF"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:3RPF"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3RPF"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3RPF"
FT HELIX 52..68
FT /evidence="ECO:0007829|PDB:3RPF"
FT STRAND 71..83
FT /evidence="ECO:0007829|PDB:3RPF"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:3RPF"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:3RPF"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3RPF"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3RPF"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3RPF"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:3RPF"
SQ SEQUENCE 145 AA; 16627 MW; D1DCD65D54AC9231 CRC64;
MLKIIQGALD TRELLKAYQE EACAKNFGAF CVFVGIVRKE DNIQGLSFDI YEALLKTWFE
KWHHKAKDLG VVLKMAHSLG DVLIGQSSFL CVSMGKNRKN ALELYENFIE DFKHNAPIWK
YDLIHNKRIY AKERSHPLKG SGLLA
