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 04-FEB-2015, entry version 141.
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; FALAPKD; -.
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 Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0061598; F:molybdopterin adenylyltransferase activity; IBA:GO_Central.
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
//
