MOAD_ECOLI
ID MOAD_ECOLI Reviewed; 81 AA.
AC P30748; P77422;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 186.
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; Synonyms=chlA4, chlM; OrderedLocusNames=b0784, JW0767;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 1-15, CHARACTERIZATION, MASS SPECTROMETRY, AND
RP IDENTIFICATION OF THIOCARBOXYLATE.
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 AMPYLATION AT GLY-81, INTERACTION WITH MOEB, AND MASS SPECTROMETRY.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=11463785; DOI=10.1074/jbc.m102787200;
RA Leimkuehler S., Wuebbens M.M., Rajagopalan K.V.;
RT "Characterization of Escherichia coli MoeB and its involvement in the
RT activation of molybdopterin synthase for the biosynthesis of the molybdenum
RT cofactor.";
RL J. Biol. Chem. 276:34695-34701(2001).
RN [7]
RP FUNCTION.
RX PubMed=17223713; DOI=10.1021/bi062011w;
RA Schmitz J., Wuebbens M.M., Rajagopalan K.V., Leimkuehler S.;
RT "Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a
RT molybdenum cofactor biosynthesis protein with a ubiquitin fold.";
RL Biochemistry 46:909-916(2007).
RN [8]
RP IDENTIFICATION OF ISCS AS SULFUR DONOR, AND INTERACTION WITH ISCS.
RX PubMed=19946146; DOI=10.1074/jbc.m109.082172;
RA Zhang W., Urban A., Mihara H., Leimkuehler S., Kurihara T., Esaki N.;
RT "IscS functions as a primary sulfur-donating enzyme by interacting
RT specifically with MoeB and MoaD in the biosynthesis of molybdopterin in
RT Escherichia coli.";
RL J. Biol. Chem. 285:2302-2308(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEXES WITH MOAE,
RP CROSS-LINKING TO MOAE, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH MOEB; ZINC; ATP AND
RP IN AN ADENYLATE FORM, AND COVALENT BINDING OF AMP.
RX PubMed=11713534; DOI=10.1038/35104586;
RA Lake M.W., Wuebbens M.M., Rajagopalan K.V., Schindelin H.;
RT "Mechanism of ubiquitin activation revealed by the structure of a bacterial
RT MoeB-MoaD complex.";
RL Nature 414:325-329(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF THIOCARBOXYLATE FORM IN COMPLEX
RP WITH MOAE, THIOCARBOXYLATION AT GLY-81, 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: Involved in sulfur transfer in the conversion of
CC molybdopterin precursor Z to molybdopterin.
CC {ECO:0000269|PubMed:17223713}.
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. {ECO:0000269|PubMed:11135669,
CC ECO:0000269|PubMed:12571227}.
CC -!- INTERACTION:
CC P30748; P30749: moaE; NbExp=8; IntAct=EBI-554366, EBI-554376;
CC P30748; P0A7K2: rplL; NbExp=2; IntAct=EBI-554366, EBI-543702;
CC -!- INDUCTION: By anaerobiosis, repressed by the molybdenum cofactor.
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:0000269|PubMed:12571227}.
CC -!- MASS SPECTROMETRY: Mass=8773.6; Mass_error=0.2; Method=Electrospray;
CC Note=The measured mass is that of the thiolated protein.;
CC Evidence={ECO:0000269|PubMed:8514782};
CC -!- MASS SPECTROMETRY: Mass=8757.0; Mass_error=1.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8514782};
CC -!- MASS SPECTROMETRY: Mass=8744; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11463785};
CC -!- MASS SPECTROMETRY: Mass=8744; Method=API;
CC Evidence={ECO:0000269|PubMed:11135669};
CC -!- MASS SPECTROMETRY: Mass=8760; Method=API; Note=The measured mass is
CC that of the thiolated protein.; 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 MoaD family. {ECO:0000305}.
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DR EMBL; X70420; CAA49864.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73871.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35442.1; -; Genomic_DNA.
DR PIR; H64814; H64814.
DR RefSeq; NP_415305.1; NC_000913.3.
DR RefSeq; WP_000598619.1; NZ_STEB01000028.1.
DR PDB; 1FM0; X-ray; 1.45 A; D=1-81.
DR PDB; 1FMA; X-ray; 1.58 A; D=1-81.
DR PDB; 1JW9; X-ray; 1.70 A; D=1-81.
DR PDB; 1JWA; X-ray; 2.90 A; D=1-81.
DR PDB; 1JWB; X-ray; 2.10 A; D=1-81.
DR PDB; 1NVI; X-ray; 1.90 A; D=1-81.
DR PDB; 3BII; X-ray; 2.50 A; D=1-81.
DR PDBsum; 1FM0; -.
DR PDBsum; 1FMA; -.
DR PDBsum; 1JW9; -.
DR PDBsum; 1JWA; -.
DR PDBsum; 1JWB; -.
DR PDBsum; 1NVI; -.
DR PDBsum; 3BII; -.
DR AlphaFoldDB; P30748; -.
DR SMR; P30748; -.
DR BioGRID; 4262177; 13.
DR BioGRID; 849772; 3.
DR ComplexPortal; CPX-1968; Molybdopterin-synthase adenylyltransferase complex.
DR ComplexPortal; CPX-1970; Molybdopterin synthase.
DR DIP; DIP-10231N; -.
DR IntAct; P30748; 16.
DR STRING; 511145.b0784; -.
DR jPOST; P30748; -.
DR PaxDb; P30748; -.
DR PRIDE; P30748; -.
DR EnsemblBacteria; AAC73871; AAC73871; b0784.
DR EnsemblBacteria; BAA35442; BAA35442; BAA35442.
DR GeneID; 66670945; -.
DR GeneID; 945398; -.
DR KEGG; ecj:JW0767; -.
DR KEGG; eco:b0784; -.
DR PATRIC; fig|1411691.4.peg.1494; -.
DR EchoBASE; EB1554; -.
DR eggNOG; COG1977; Bacteria.
DR HOGENOM; CLU_114601_4_0_6; -.
DR InParanoid; P30748; -.
DR OMA; DRVHAKP; -.
DR PhylomeDB; P30748; -.
DR BioCyc; EcoCyc:EG11597-MON; -.
DR BioCyc; MetaCyc:EG11597-MON; -.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P30748; -.
DR PRO; PR:P30748; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990133; C:molybdopterin cofactor (Moco) biosynthesis adenylyltransferase complex; IPI:ComplexPortal.
DR GO; GO:1990140; C:MPT synthase complex; IPI:ComplexPortal.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:ComplexPortal.
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; Direct protein sequencing; Isopeptide bond;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..81
FT /note="Molybdopterin synthase sulfur carrier subunit"
FT /id="PRO_0000209131"
FT MOD_RES 81
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000269|PubMed:12571227"
FT MOD_RES 81
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000269|PubMed:11463785"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-119 in MoaE)"
FT CONFLICT 9
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="A -> R (in Ref. 1; CAA49864)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1FM0"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1FM0"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:1FM0"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1FM0"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1JWB"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1FM0"
SQ SEQUENCE 81 AA; 8758 MW; 1E0A440520EE82F4 CRC64;
MIKVLFFAQV RELVGTDATE VAADFPTVEA LRQHMAAQSD RWALALEDGK LLAAVNQTLV
SFDHPLTDGD EVAFFPPVTG G
