Документ взят из кэша поисковой машины. Адрес оригинального документа : http://kodomo.cmm.msu.ru/~alexus/projects/P12282.txt
Дата изменения: Mon Feb 9 16:35:27 2009
Дата индексирования: Tue Oct 2 10:12:08 2012
Кодировка:
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 16-DEC-2008, entry version 85.
DE RecName: Full=Molybdopterin biosynthesis protein moeB;
GN Name=moeB; Synonyms=chlN; OrderedLocusNames=b0826, JW0810;
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 MEDLINE=88314906; 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 MEDLINE=97061202; 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 MEDLINE=97426617; 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 277:1453-1474(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).
CC -!- FUNCTION: Involved in the biosynthesis of a demolybdo cofactor
CC (molybdopterin), necessary for molybdoenzymes. Plays a role in the
CC activation of the small subunit of the molybdopterin converting
CC factor (moaD).
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- INTERACTION:
CC P0A6Y8:dnaK; NbExp=1; IntAct=EBI-554435, EBI-542092;
CC P30748:moaD; NbExp=1; IntAct=EBI-554435, EBI-554366;
CC -!- SIMILARITY: Belongs to the hesA/moeB/thiF family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; AP_001457.1; -.
DR RefSeq; NP_415347.1; -.
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 DIP; DIP:10241N; -.
DR IntAct; P12282; 15.
DR GeneID; 945452; -.
DR GenomeReviews; AP009048_GR; JW0810.
DR GenomeReviews; U00096_GR; b0826.
DR KEGG; ecj:JW0810; -.
DR KEGG; eco:b0826; -.
DR EchoBASE; EB0152; -.
DR EcoGene; EG10154; moeB.
DR HOGENOM; P12282; -.
DR BioCyc; EcoCyc:EG10154-MON; -.
DR BioCyc; MetaCyc:EG10154-MON; -.
DR LinkHub; P12282; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005515; F:protein binding; IPI:IntAct.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
DR InterPro; IPR007901; MoeZ_MoeB.
DR InterPro; IPR012730; Mopterin_Synthase_Sase_MoeB.
DR InterPro; IPR016040; NAD(P)-bd.
DR InterPro; IPR000594; ThiF_NAD_FAD_bd.
DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR Pfam; PF05237; MoeZ_MoeB; 1.
DR Pfam; PF00899; ThiF; 1.
DR TIGRFAMs; TIGR02355; moeB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Molybdenum cofactor biosynthesis.
FT CHAIN 1 249 Molybdopterin biosynthesis protein moeB.
FT /FTId=PRO_0000120575.
FT HELIX 6 11
FT HELIX 13 16
FT TURN 19 21
FT HELIX 22 31
FT STRAND 33 37
FT HELIX 41 53
FT STRAND 56 61
FT HELIX 68 72
FT HELIX 79 81
FT HELIX 86 97
FT STRAND 101 106
FT HELIX 112 120
FT STRAND 122 127
FT HELIX 132 145
FT STRAND 149 156
FT STRAND 158 164
FT HELIX 173 177
FT HELIX 194 213
FT STRAND 220 227
FT TURN 228 231
FT STRAND 232 237
FT TURN 245 247
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
//