MOAE_ECOLI
ID MOAE_ECOLI Reviewed; 150 AA.
AC P30749;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
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; Synonyms=chlA5; OrderedLocusNames=b0785, JW0768;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8361352; DOI=10.1111/j.1365-2958.1993.tb01652.x;
RA Rivers S.L., McNairn E., Blasco F., Giordano G., Boxer D.H.;
RT "Molecular genetic analysis of the moa operon of Escherichia coli K-12
RT required for molybdenum cofactor biosynthesis.";
RL Mol. Microbiol. 8:1071-1081(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION, AND MASS SPECTROMETRY.
RX PubMed=8514782; DOI=10.1016/s0021-9258(19)38677-6;
RA Pitterle D.M., Rajagopalan K.V.;
RT "The biosynthesis of molybdopterin in Escherichia coli. Purification and
RT characterization of the converting factor.";
RL J. Biol. Chem. 268:13499-13505(1993).
RN [6]
RP CATALYTIC ACTIVITY, KINETIC ANALYSIS, DISCOVERY OF REACTION INTERMEDIATE,
RP AND MUTAGENESIS OF PHE-34; ARG-39; MET-115; LYS-119; LYS-126; GLU-128 AND
RP ARG-140.
RX PubMed=12571226; DOI=10.1074/jbc.m300453200;
RA Wuebbens M.M., Rajagopalan K.V.;
RT "Mechanistic and mutational studies of Escherichia coli molybdopterin
RT synthase clarify the final step of molybdopterin biosynthesis.";
RL J. Biol. Chem. 278:14523-14532(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEXES WITH MOAD,
RP CROSS-LINKING TO MOAD, MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=11135669; DOI=10.1038/83034;
RA Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H.;
RT "Crystal structure of molybdopterin synthase and its evolutionary
RT relationship to ubiquitin activation.";
RL Nat. Struct. Biol. 8:42-46(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP MOAD-THIOCARBOXYLATE, AND REACTION MECHANISM.
RX PubMed=12571227; DOI=10.1074/jbc.m300449200;
RA Rudolph M.J., Wuebbens M.M., Turque O., Rajagopalan K.V., Schindelin H.;
RT "Structural studies of molybdopterin synthase provide insights into its
RT catalytic mechanism.";
RL J. Biol. Chem. 278:14514-14522(2003).
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:12571226};
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. {ECO:0000269|PubMed:11135669, ECO:0000269|PubMed:12571227}.
CC -!- INTERACTION:
CC P30749; P30748: moaD; NbExp=8; IntAct=EBI-554376, EBI-554366;
CC P30749; P32125: mobB; NbExp=2; IntAct=EBI-554376, EBI-879965;
CC -!- INDUCTION: By anaerobiosis, repressed by the molybdenum cofactor.
CC -!- MASS SPECTROMETRY: Mass=16849.7; Mass_error=0.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8514782};
CC -!- MASS SPECTROMETRY: Mass=16851; Method=API;
CC Evidence={ECO:0000269|PubMed:11135669};
CC -!- MISCELLANEOUS: The cross-link is not seen in all structures of the
CC MoaE-MoaD complex.
CC -!- SIMILARITY: Belongs to the MoaE family. {ECO:0000305}.
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DR EMBL; X70420; CAA49865.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73872.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35443.1; -; Genomic_DNA.
DR PIR; S35002; S31883.
DR RefSeq; NP_415306.1; NC_000913.3.
DR RefSeq; WP_000852296.1; NZ_SSZK01000002.1.
DR PDB; 1FM0; X-ray; 1.45 A; E=1-150.
DR PDB; 1FMA; X-ray; 1.58 A; E=1-150.
DR PDB; 1NVI; X-ray; 1.90 A; E=1-150.
DR PDB; 1NVJ; X-ray; 2.15 A; A/B/C/D/E/F=1-140.
DR PDB; 3BII; X-ray; 2.50 A; E=2-150.
DR PDBsum; 1FM0; -.
DR PDBsum; 1FMA; -.
DR PDBsum; 1NVI; -.
DR PDBsum; 1NVJ; -.
DR PDBsum; 3BII; -.
DR AlphaFoldDB; P30749; -.
DR SMR; P30749; -.
DR BioGRID; 4262180; 17.
DR BioGRID; 849773; 10.
DR ComplexPortal; CPX-1970; Molybdopterin synthase.
DR DIP; DIP-10232N; -.
DR IntAct; P30749; 21.
DR STRING; 511145.b0785; -.
DR DrugBank; DB01942; Formic acid.
DR jPOST; P30749; -.
DR PaxDb; P30749; -.
DR PRIDE; P30749; -.
DR EnsemblBacteria; AAC73872; AAC73872; b0785.
DR EnsemblBacteria; BAA35443; BAA35443; BAA35443.
DR GeneID; 945399; -.
DR KEGG; ecj:JW0768; -.
DR KEGG; eco:b0785; -.
DR PATRIC; fig|1411691.4.peg.1493; -.
DR EchoBASE; EB1555; -.
DR eggNOG; COG0314; Bacteria.
DR HOGENOM; CLU_089568_2_1_6; -.
DR InParanoid; P30749; -.
DR OMA; WPLQRVS; -.
DR PhylomeDB; P30749; -.
DR BioCyc; EcoCyc:EG11598-MON; -.
DR BioCyc; MetaCyc:EG11598-MON; -.
DR BRENDA; 2.8.1.12; 2026.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P30749; -.
DR PRO; PR:P30749; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990140; C:MPT synthase complex; IPI:ComplexPortal.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:ComplexPortal.
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; Direct protein sequencing; Isopeptide bond;
KW Molybdenum cofactor biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8361352,
FT ECO:0000269|PubMed:8514782"
FT CHAIN 2..150
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163082"
FT BINDING 37..39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in MoaD)"
FT MUTAGEN 34
FT /note="F->A: 4-fold lower activity than wild-type."
FT /evidence="ECO:0000269|PubMed:12571226"
FT MUTAGEN 39
FT /note="R->A: 24-fold lower activity than wild-type."
FT /evidence="ECO:0000269|PubMed:12571226"
FT MUTAGEN 115
FT /note="M->A: 4-fold lower activity than wild-type."
FT /evidence="ECO:0000269|PubMed:12571226"
FT MUTAGEN 119
FT /note="K->A: No activity."
FT /evidence="ECO:0000269|PubMed:12571226"
FT MUTAGEN 126
FT /note="K->A: 58-fold lower activity than wild-type.
FT Accumulates large quantities of reaction intermediate."
FT /evidence="ECO:0000269|PubMed:12571226"
FT MUTAGEN 128
FT /note="E->K: 17-fold lower activity than wild-type."
FT /evidence="ECO:0000269|PubMed:12571226"
FT MUTAGEN 140
FT /note="R->A: 2-fold lower activity than wild-type."
FT /evidence="ECO:0000269|PubMed:12571226"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1FM0"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1FM0"
FT HELIX 56..73
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:1FM0"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1FM0"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:1FM0"
SQ SEQUENCE 150 AA; 16981 MW; 6E40776E5A6E85BB CRC64;
MAETKIVVGP QPFSVGEEYP WLAERDEDGA VVTFTGKVRN HNLGDSVNAL TLEHYPGMTE
KALAEIVDEA RNRWPLGRVT VIHRIGELWP GDEIVFVGVT SAHRSSAFEA GQFIMDYLKT
RAPFWKREAT PEGDRWVEAR ESDQQAAKRW
