MOEB_ECOLI
ID MOEB_ECOLI Reviewed; 249 AA.
AC P12282;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Molybdopterin-synthase adenylyltransferase;
DE EC=2.7.7.80;
DE AltName: Full=MoaD protein adenylase;
DE AltName: Full=Molybdopterin-converting factor subunit 1 adenylase;
DE AltName: Full=Sulfur carrier protein MoaD adenylyltransferase;
GN Name=moeB; Synonyms=chlN; OrderedLocusNames=b0826, JW0810;
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 / W3110 / ZK126;
RX PubMed=3045084; DOI=10.1128/jb.170.9.4097-4102.1988;
RA Nohno T., Kasai Y., Saito T.;
RT "Cloning and sequencing of the Escherichia coli chlEN operon involved in
RT molybdopterin biosynthesis.";
RL J. Bacteriol. 170:4097-4102(1988).
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 FUNCTION, AND SULFUR DONOR.
RX PubMed=11290749; DOI=10.1074/jbc.m102072200;
RA Leimkuehler S., Rajagopalan K.V.;
RT "A sulfurtransferase is required in the transfer of cysteine sulfur in the
RT in vitro synthesis of molybdopterin from precursor Z in Escherichia coli.";
RL J. Biol. Chem. 276:22024-22031(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, INTERACTION WITH MOAD,
RP MUTAGENESIS OF CYS-44; CYS-128; CYS-142; CYS-172; CYS-175; CYS-187;
RP CYS-231; CYS-244 AND CYS-247, 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 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH MOAD; ZINC; MOAD
RP AND ATP AND MOAD-ADENYLATE, MUTAGENESIS OF ARG-14; ARG-73 AND ASP-130, AND
RP REACTION MECHANISM.
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).
CC -!- FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the
CC C-terminal glycine of sulfur carrier protein MoaD.
CC {ECO:0000269|PubMed:11290749, ECO:0000269|PubMed:11463785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier
CC protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616,
CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618,
CC ChEBI:CHEBI:90778; EC=2.7.7.80;
CC Evidence={ECO:0000269|PubMed:11463785};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11463785};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11463785};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homodimer. Forms a stable heterotetrameric complex of 2 MoeB
CC and 2 MoaD during adenylation of MoaD. {ECO:0000269|PubMed:11463785}.
CC -!- INTERACTION:
CC P12282; P0A6Y8: dnaK; NbExp=2; IntAct=EBI-554435, EBI-542092;
CC -!- MASS SPECTROMETRY: Mass=26563; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11463785};
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR EMBL; M21151; AAA23580.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73913.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35514.1; -; Genomic_DNA.
DR PIR; B32352; B32352.
DR RefSeq; NP_415347.1; NC_000913.3.
DR RefSeq; WP_000829217.1; NZ_SSZK01000002.1.
DR PDB; 1JW9; X-ray; 1.70 A; B=1-249.
DR PDB; 1JWA; X-ray; 2.90 A; B=1-249.
DR PDB; 1JWB; X-ray; 2.10 A; B=1-249.
DR PDBsum; 1JW9; -.
DR PDBsum; 1JWA; -.
DR PDBsum; 1JWB; -.
DR AlphaFoldDB; P12282; -.
DR SMR; P12282; -.
DR BioGRID; 4261831; 11.
DR ComplexPortal; CPX-1968; Molybdopterin-synthase adenylyltransferase complex.
DR DIP; DIP-10241N; -.
DR IntAct; P12282; 15.
DR STRING; 511145.b0826; -.
DR jPOST; P12282; -.
DR PaxDb; P12282; -.
DR PRIDE; P12282; -.
DR EnsemblBacteria; AAC73913; AAC73913; b0826.
DR EnsemblBacteria; BAA35514; BAA35514; BAA35514.
DR GeneID; 945452; -.
DR KEGG; ecj:JW0810; -.
DR KEGG; eco:b0826; -.
DR PATRIC; fig|1411691.4.peg.1452; -.
DR EchoBASE; EB0152; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_10_3_6; -.
DR InParanoid; P12282; -.
DR OMA; MIYDALE; -.
DR PhylomeDB; P12282; -.
DR BioCyc; EcoCyc:EG10154-MON; -.
DR BioCyc; MetaCyc:EG10154-MON; -.
DR BRENDA; 2.7.7.80; 2026.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P12282; -.
DR PRO; PR:P12282; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990133; C:molybdopterin cofactor (Moco) biosynthesis adenylyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:ComplexPortal.
DR InterPro; IPR012730; Mopterin_Synthase_Sase_MoeB.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR TIGRFAMs; TIGR02355; moeB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Metal-binding; Molybdenum cofactor biosynthesis;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..249
FT /note="Molybdopterin-synthase adenylyltransferase"
FT /id="PRO_0000120575"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 69..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 130..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 14
FT /note="R->A,K: No effect."
FT /evidence="ECO:0000269|PubMed:11713534"
FT MUTAGEN 14
FT /note="R->A: No activity; when associated with A-73."
FT /evidence="ECO:0000269|PubMed:11713534"
FT MUTAGEN 44
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 73
FT /note="R->A: No effect. No activity; when associated with
FT A-14."
FT /evidence="ECO:0000269|PubMed:11713534"
FT MUTAGEN 73
FT /note="R->K: Substantially reduced activity."
FT /evidence="ECO:0000269|PubMed:11713534"
FT MUTAGEN 128
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 128
FT /note="C->Y: No activity."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 130
FT /note="D->A: No activity."
FT /evidence="ECO:0000269|PubMed:11713534"
FT MUTAGEN 130
FT /note="D->E: Substantially reduced activity."
FT /evidence="ECO:0000269|PubMed:11713534"
FT MUTAGEN 142
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 172
FT /note="C->A: No zinc bound and no enzyme activity."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 175
FT /note="C->A: No zinc bound and no enzyme activity."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 187
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 231
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 244
FT /note="C->A: No zinc bound and almost no enzyme activity."
FT /evidence="ECO:0000269|PubMed:11463785"
FT MUTAGEN 247
FT /note="C->A: No zinc bound and almost no enzyme activity."
FT /evidence="ECO:0000269|PubMed:11463785"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:1JW9"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:1JW9"
FT HELIX 194..213
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:1JW9"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:1JW9"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1JW9"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1JW9"
SQ SEQUENCE 249 AA; 26719 MW; 12C77082B3F39D7D CRC64;
MAELSDQEML RYNRQIILRG FDFDGQEALK DSRVLIVGLG GLGCAASQYL ASAGVGNLTL
LDFDTVSLSN LQRQTLHSDA TVGQPKVESA RDALTRINPH IAITPVNALL DDAELAALIA
EHDLVLDCTD NVAVRNQLNA GCFAAKVPLV SGAAIRMEGQ ITVFTYQDGE PCYRCLSRLF
GENALTCVEA GVMAPLIGVI GSLQAMEAIK MLAGYGKPAS GKIVMYDAMT CQFREMKLMR
NPGCEVCGQ
