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Database: UniProt
Entry: P12281
LinkDB: P12281
Original site: P12281 
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   26-NOV-2014, entry version 139.
DE   RecName: Full=Molybdopterin molybdenumtransferase;
DE            Short=MPT Mo-transferase;
DE            EC=2.10.1.1;
GN   Name=moeA; Synonyms=bisB, chlE, narE; OrderedLocusNames=b0827, JW0811;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3045084;
RA   Nohno T., Kasai Y., Saito T.;
RT   "Cloning and sequencing of the Escherichia coli chlEN operon involved
RT   in 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.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9515915;
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
RT   stages of molybdenum cofactor biosynthesis in Escherichia coli.";
RL   J. Biol. Chem. 277:48199-48204(2002).
RN   [7]
RP   FUNCTION AS MPT--MO LIGASE.
RX   PubMed=15632135; DOI=10.1074/jbc.M413783200;
RA   Nichols J.D., Rajagopalan K.V.;
RT   "In vitro molybdenum ligation to molybdopterin using purified
RT   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.,
RA   Larocque R., 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
RT   to the 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: Adenylyl-molybdopterin + molybdate =
CC       molybdenum cofactor + AMP.
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.
CC       {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       P32173:mobA; NbExp=3; IntAct=EBI-554393, EBI-1133881;
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; YP_489100.1; NC_007779.1.
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   ProteinModelPortal; P12281; -.
DR   SMR; P12281; 5-408.
DR   DIP; DIP-10240N; -.
DR   IntAct; P12281; 8.
DR   MINT; MINT-1250871; -.
DR   STRING; 511145.b0827; -.
DR   PaxDb; P12281; -.
DR   PRIDE; P12281; -.
DR   EnsemblBacteria; AAC73914; AAC73914; b0827.
DR   EnsemblBacteria; BAA35515; BAA35515; BAA35515.
DR   GeneID; 12930985; -.
DR   GeneID; 945454; -.
DR   KEGG; ecj:Y75_p0800; -.
DR   KEGG; eco:b0827; -.
DR   PATRIC; 32116857; VBIEscCol129921_0854.
DR   EchoBASE; EB0151; -.
DR   EcoGene; EG10153; moeA.
DR   eggNOG; COG0303; -.
DR   HOGENOM; HOG000280652; -.
DR   InParanoid; P12281; -.
DR   KO; K03750; -.
DR   OMA; QMLDRIS; -.
DR   OrthoDB; EOG66MQMC; -.
DR   PhylomeDB; P12281; -.
DR   BioCyc; EcoCyc:EG10153-MONOMER; -.
DR   BioCyc; ECOL316407:JW0811-MONOMER; -.
DR   BioCyc; MetaCyc:EG10153-MONOMER; -.
DR   BioCyc; RETL1328306-WGS:GSTH-2187-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   EvolutionaryTrace; P12281; -.
DR   PRO; PR:P12281; -.
DR   Genevestigator; P12281; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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   Gene3D; 2.40.340.10; -; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR020817; Mo_cofactor_synthesis.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR001453; Mopterin-bd_dom.
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; Complete proteome; Magnesium; Metal-binding; Molybdenum;
KW   Molybdenum cofactor biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    411       Molybdopterin molybdenumtransferase.
FT                                /FTId=PRO_0000170989.
FT   HELIX        10     20       {ECO:0000244|PDB:1G8L}.
FT   STRAND       27     31       {ECO:0000244|PDB:1G8L}.
FT   HELIX        32     34       {ECO:0000244|PDB:1G8L}.
FT   STRAND       39     42       {ECO:0000244|PDB:1G8L}.
FT   STRAND       50     53       {ECO:0000244|PDB:1G8L}.
FT   STRAND       55     63       {ECO:0000244|PDB:1G8L}.
FT   HELIX        65     70       {ECO:0000244|PDB:1G8L}.
FT   STRAND       76     81       {ECO:0000244|PDB:1G8L}.
FT   STRAND       82     84       {ECO:0000244|PDB:1FC5}.
FT   STRAND       95     98       {ECO:0000244|PDB:1G8L}.
FT   STRAND      110    113       {ECO:0000244|PDB:1G8L}.
FT   HELIX       114    116       {ECO:0000244|PDB:1G8L}.
FT   STRAND      117    120       {ECO:0000244|PDB:1G8L}.
FT   STRAND      123    126       {ECO:0000244|PDB:1G8L}.
FT   TURN        132    135       {ECO:0000244|PDB:1G8L}.
FT   STRAND      141    143       {ECO:0000244|PDB:1G8L}.
FT   STRAND      147    150       {ECO:0000244|PDB:1G8L}.
FT   TURN        158    160       {ECO:0000244|PDB:1G8L}.
FT   HELIX       161    166       {ECO:0000244|PDB:1G8L}.
FT   STRAND      171    175       {ECO:0000244|PDB:1G8L}.
FT   STRAND      179    185       {ECO:0000244|PDB:1G8L}.
FT   STRAND      187    190       {ECO:0000244|PDB:2NRP}.
FT   STRAND      192    194       {ECO:0000244|PDB:2NQV}.
FT   HELIX       205    215       {ECO:0000244|PDB:1G8L}.
FT   STRAND      219    226       {ECO:0000244|PDB:1G8L}.
FT   HELIX       230    243       {ECO:0000244|PDB:1G8L}.
FT   STRAND      245    249       {ECO:0000244|PDB:1G8L}.
FT   STRAND      251    253       {ECO:0000244|PDB:1G8L}.
FT   STRAND      255    257       {ECO:0000244|PDB:1G8L}.
FT   HELIX       260    268       {ECO:0000244|PDB:1G8L}.
FT   STRAND      269    280       {ECO:0000244|PDB:1G8L}.
FT   STRAND      283    288       {ECO:0000244|PDB:1G8L}.
FT   STRAND      290    296       {ECO:0000244|PDB:1G8L}.
FT   HELIX       301    310       {ECO:0000244|PDB:1G8L}.
FT   HELIX       312    320       {ECO:0000244|PDB:1G8L}.
FT   STRAND      326    328       {ECO:0000244|PDB:2NQM}.
FT   STRAND      331    337       {ECO:0000244|PDB:1G8L}.
FT   STRAND      345    355       {ECO:0000244|PDB:1G8L}.
FT   STRAND      357    359       {ECO:0000244|PDB:2NQM}.
FT   STRAND      361    365       {ECO:0000244|PDB:1G8L}.
FT   HELIX       376    379       {ECO:0000244|PDB:1G8L}.
FT   STRAND      381    386       {ECO:0000244|PDB:1G8L}.
FT   STRAND      398    403       {ECO:0000244|PDB:1G8L}.
FT   HELIX       406    408       {ECO:0000244|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
//
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