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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   01-OCT-2014, entry version 137.
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: Binds 1 magnesium 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   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:0005515; F:protein binding; IPI:IntAct.
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
FT   STRAND       27     31
FT   HELIX        32     34
FT   STRAND       39     42
FT   STRAND       50     53
FT   STRAND       55     63
FT   HELIX        65     70
FT   STRAND       76     81
FT   STRAND       82     84
FT   STRAND       95     98
FT   STRAND      110    113
FT   HELIX       114    116
FT   STRAND      117    120
FT   STRAND      123    126
FT   TURN        132    135
FT   STRAND      141    143
FT   STRAND      147    150
FT   TURN        158    160
FT   HELIX       161    166
FT   STRAND      171    175
FT   STRAND      179    185
FT   STRAND      187    190
FT   STRAND      192    194
FT   HELIX       205    215
FT   STRAND      219    226
FT   HELIX       230    243
FT   STRAND      245    249
FT   STRAND      251    253
FT   STRAND      255    257
FT   HELIX       260    268
FT   STRAND      269    280
FT   STRAND      283    288
FT   STRAND      290    296
FT   HELIX       301    310
FT   HELIX       312    320
FT   STRAND      326    328
FT   STRAND      331    337
FT   STRAND      345    355
FT   STRAND      357    359
FT   STRAND      361    365
FT   HELIX       376    379
FT   STRAND      381    386
FT   STRAND      398    403
FT   HELIX       406    408
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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