MOEA_ECOLI
ID MOEA_ECOLI Reviewed; 411 AA.
AC P12281;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Molybdopterin molybdenumtransferase;
DE Short=MPT Mo-transferase;
DE EC=2.10.1.1 {ECO:0000269|PubMed:15632135};
GN Name=moeA; Synonyms=bisB, chlE, narE; OrderedLocusNames=b0827, JW0811;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 CHARACTERIZATION.
RX PubMed=9515915; DOI=10.1128/jb.180.6.1466-1472.1998;
RA Hasona A., Ray R.M., Shanmugam K.T.;
RT "Physiological and genetic analyses leading to identification of a
RT biochemical role for the moeA (molybdate metabolism) gene product in
RT Escherichia coli.";
RL J. Bacteriol. 180:1466-1472(1998).
RN [6]
RP INTERACTION WITH MOBA; MOGA AND MOBB.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12372836; DOI=10.1074/jbc.m205806200;
RA Magalon A., Frixon C., Pommier J., Giordano G., Blasco F.;
RT "In vivo interactions between gene products involved in the final stages of
RT molybdenum cofactor biosynthesis in Escherichia coli.";
RL J. Biol. Chem. 277:48199-48204(2002).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15632135; DOI=10.1074/jbc.m413783200;
RA Nichols J.D., Rajagopalan K.V.;
RT "In vitro molybdenum ligation to molybdopterin using purified components.";
RL J. Biol. Chem. 280:7817-7822(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION,
RP SUBUNIT, AND COFACTOR.
RX PubMed=11428898; DOI=10.1006/jmbi.2001.4771;
RA Schrag J.D., Huang W., Sivaraman J., Smith C., Plamondon J., Larocque R.,
RA Matte A., Cygler M.;
RT "The crystal structure of Escherichia coli MoeA, a protein from the
RT molybdopterin synthesis pathway.";
RL J. Mol. Biol. 310:419-431(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND SUBUNIT.
RX PubMed=11525167; DOI=10.1016/s0969-2126(01)00588-3;
RA Xiang S., Nichols J., Rajagopalan K.V., Schindelin H.;
RT "The crystal structure of Escherichia coli MoeA and its relationship to the
RT multifunctional protein gephyrin.";
RL Structure 9:299-310(2001).
CC -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC molybdopterin with the concomitant release of AMP.
CC {ECO:0000269|PubMed:15632135}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC Evidence={ECO:0000269|PubMed:15632135};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11428898};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:11428898};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homodimer. Interacts with MobA, MogA and MobB in vivo.
CC {ECO:0000269|PubMed:11428898, ECO:0000269|PubMed:11525167,
CC ECO:0000269|PubMed:12372836}.
CC -!- INTERACTION:
CC P12281; P32173: mobA; NbExp=3; IntAct=EBI-554393, EBI-1133881;
CC P12281; P12281: moeA; NbExp=5; IntAct=EBI-554393, EBI-554393;
CC P12281; P0A796: pfkA; NbExp=2; IntAct=EBI-554393, EBI-554405;
CC -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000305}.
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DR EMBL; M21151; AAA23579.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73914.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35515.1; -; Genomic_DNA.
DR PIR; A32352; A32352.
DR RefSeq; NP_415348.1; NC_000913.3.
DR RefSeq; WP_000397340.1; NZ_SSZK01000002.1.
DR PDB; 1FC5; X-ray; 2.20 A; A/B=1-411.
DR PDB; 1G8L; X-ray; 1.95 A; A/B=1-411.
DR PDB; 1G8R; X-ray; 2.65 A; A/B=1-411.
DR PDB; 2NQK; X-ray; 2.90 A; A/B=1-411.
DR PDB; 2NQM; X-ray; 3.00 A; A/B=1-411.
DR PDB; 2NQN; X-ray; 2.20 A; A/B=1-411.
DR PDB; 2NQQ; X-ray; 2.40 A; A/B/C/D=1-411.
DR PDB; 2NQR; X-ray; 2.20 A; A/B=1-411.
DR PDB; 2NQS; X-ray; 2.50 A; A/B=1-411.
DR PDB; 2NQU; X-ray; 2.70 A; A/B=1-411.
DR PDB; 2NQV; X-ray; 2.82 A; A/B=1-411.
DR PDB; 2NRO; X-ray; 2.50 A; A/B=1-411.
DR PDB; 2NRP; X-ray; 3.00 A; A/B=1-411.
DR PDB; 2NRS; X-ray; 2.80 A; A/B=1-411.
DR PDBsum; 1FC5; -.
DR PDBsum; 1G8L; -.
DR PDBsum; 1G8R; -.
DR PDBsum; 2NQK; -.
DR PDBsum; 2NQM; -.
DR PDBsum; 2NQN; -.
DR PDBsum; 2NQQ; -.
DR PDBsum; 2NQR; -.
DR PDBsum; 2NQS; -.
DR PDBsum; 2NQU; -.
DR PDBsum; 2NQV; -.
DR PDBsum; 2NRO; -.
DR PDBsum; 2NRP; -.
DR PDBsum; 2NRS; -.
DR AlphaFoldDB; P12281; -.
DR SMR; P12281; -.
DR BioGRID; 4259979; 41.
DR BioGRID; 849828; 1.
DR DIP; DIP-10240N; -.
DR IntAct; P12281; 8.
DR STRING; 511145.b0827; -.
DR jPOST; P12281; -.
DR PaxDb; P12281; -.
DR PRIDE; P12281; -.
DR EnsemblBacteria; AAC73914; AAC73914; b0827.
DR EnsemblBacteria; BAA35515; BAA35515; BAA35515.
DR GeneID; 945454; -.
DR KEGG; ecj:JW0811; -.
DR KEGG; eco:b0827; -.
DR PATRIC; fig|1411691.4.peg.1451; -.
DR EchoBASE; EB0151; -.
DR eggNOG; COG0303; Bacteria.
DR HOGENOM; CLU_010186_7_0_6; -.
DR InParanoid; P12281; -.
DR OMA; MTGAMVP; -.
DR PhylomeDB; P12281; -.
DR BioCyc; EcoCyc:EG10153-MON; -.
DR BioCyc; MetaCyc:EG10153-MON; -.
DR BRENDA; 2.10.1.1; 2026.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P12281; -.
DR PRO; PR:P12281; -.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IDA:EcoCyc.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:EcoCyc.
DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IDA:EcoCyc.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR CDD; cd00887; MoeA; 1.
DR Gene3D; 2.40.340.10; -; 1.
DR Gene3D; 3.40.980.10; -; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192; PTHR10192; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; SSF53218; 1.
DR SUPFAM; SSF63867; SSF63867; 1.
DR SUPFAM; SSF63882; SSF63882; 1.
DR TIGRFAMs; TIGR00177; molyb_syn; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Molybdenum;
KW Molybdenum cofactor biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..411
FT /note="Molybdopterin molybdenumtransferase"
FT /id="PRO_0000170989"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1FC5"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1G8L"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1G8L"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2NRP"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2NQV"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 269..280
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:2NQM"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:2NQM"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:1G8L"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:1G8L"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:1G8L"
SQ SEQUENCE 411 AA; 44067 MW; 6DBBC2B4191F5951 CRC64;
MEFTTGLMSL DTALNEMLSR VTPLTAQETL PLVQCFGRIL ASDVVSPLDV PGFDNSAMDG
YAVRLADIAS GQPLPVAGKS FAGQPYHGEW PAGTCIRIMT GAPVPEGCEA VVMQEQTEQM
DNGVRFTAEV RSGQNIRRRG EDISAGAVVF PAGTRLTTAE LPVIASLGIA EVPVIRKVRV
ALFSTGDELQ LPGQPLGDGQ IYDTNRLAVH LMLEQLGCEV INLGIIRDDP HALRAAFIEA
DSQADVVISS GGVSVGEADY TKTILEELGE IAFWKLAIKP GKPFAFGKLS NSWFCGLPGN
PVSATLTFYQ LVQPLLAKLS GNTASGLPAR QRVRTASRLK KTPGRLDFQR GVLQRNADGE
LEVTTTGHQG SHIFSSFSLG NCFIVLERDR GNVEVGEWVE VEPFNALFGG L
