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Дата изменения: Sat Oct 18 23:19:23 2008
Дата индексирования: Wed Jan 14 01:00:19 2009
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ID PYRD_ECOLI Reviewed; 336 AA.
AC P0A7E1; P05021;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 22-JUL-2008, entry version 40.
DE RecName: Full=Dihydroorotate dehydrogenase;
DE EC=1.3.3.1;
DE AltName: Full=Dihydroorotate oxidase;
DE AltName: Full=DHOdehase;
DE Short=DHODase;
DE Short=DHOD;
GN Name=pyrD; OrderedLocusNames=b0945, JW0928;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7.
RX MEDLINE=85285014; PubMed=2992959;
RA Larsen N.J., Jensen K.F.;
RT "Nucleotide sequence of the pyrD gene of Escherichia coli and
RT characterization of the flavoprotein dihydroorotate dehydrogenase.";
RL Eur. J. Biochem. 151:59-65(1985).
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX MEDLINE=22210214; PubMed=12220493; DOI=10.1016/S0969-2126(02)00831-6;
RA Noerager S., Jensen K.F., Bjoernberg O., Larsen S.;
RT "E. coli dihydroorotate dehydrogenase reveals structural and
RT functional distinctions between different classes of dihydroorotate
RT dehydrogenases.";
RL Structure 10:1211-1223(2002).
CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + O(2) = orotate +
CC H(2)O(2).
CC -!- COFACTOR: Binds 1 FMN per subunit.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; UMP from HCO(3)(-): step 4/6.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC Type 2 subfamily.
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DR EMBL; X02826; CAA26594.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74031.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35700.1; -; Genomic_DNA.
DR PIR; A23109; DEECDO.
DR RefSeq; AP_001575.1; -.
DR RefSeq; NP_415465.1; -.
DR PDB; 1F76; X-ray; 2.50 A; A/B/D/E=1-336.
DR PDBsum; 1F76; -.
DR IntAct; P0A7E1; -.
DR SWISS-2DPAGE; P0A7E1; -.
DR GeneID; 945556; -.
DR GenomeReviews; U00096_GR; b0945.
DR GenomeReviews; AP009048_GR; JW0928.
DR KEGG; ecj:JW0928; -.
DR KEGG; eco:b0945; -.
DR EchoBASE; EB0800; -.
DR EcoGene; EG10807; pyrD.
DR HOGENOM; P0A7E1; -.
DR BioCyc; EcoCyc:DIHYDROOROTOX-MON; -.
DR GO; GO:0005886; C:plasma membrane; IEA:HAMAP.
DR GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:HAMAP.
DR HAMAP; MF_00225; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012135; DHO_DHase_1_2.
DR InterPro; IPR005719; DHO_DHase_2.
DR InterPro; IPR001295; Dihydroorotate_DHase_core.
DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR PIRSF; PIRSF000164; DHO_oxidase; 1.
DR TIGRFAMs; TIGR01036; pyrD_sub2; 1.
DR PROSITE; PS00911; DHODEHASE_1; 1.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Complete proteome;
KW Direct protein sequencing; Flavoprotein; FMN; Membrane;
KW Oxidoreductase; Pyrimidine biosynthesis.
FT CHAIN 1 336 Dihydroorotate dehydrogenase.
FT /FTId=PRO_0000148437.
FT ACT_SITE 175 175 Nucleophile.
FT HELIX 3 10
FT HELIX 15 29
FT HELIX 33 37
FT STRAND 47 49
FT STRAND 52 60
FT HELIX 71 76
FT STRAND 80 87
FT STRAND 100 103
FT TURN 104 107
FT STRAND 108 111
FT HELIX 120 129
FT STRAND 134 140
FT HELIX 148 151
FT HELIX 152 162
FT HELIX 163 165
FT STRAND 167 172
FT STRAND 176 178
FT HELIX 181 185
FT HELIX 187 208
FT STRAND 214 217
FT HELIX 224 236
FT STRAND 240 244
FT TURN 258 261
FT STRAND 263 268
FT HELIX 269 271
FT HELIX 272 286
FT STRAND 292 297
FT HELIX 301 310
FT STRAND 313 318
FT HELIX 319 324
FT HELIX 326 335
SQ SEQUENCE 336 AA; 36775 MW; 973227EAE6B83622 CRC64;
MYYPFVRKAL FQLDPERAHE FTFQQLRRIT GTPFEALVRQ KVPAKPVNCM GLTFKNPLGL
AAGLDKDGEC IDALGAMGFG SIEIGTVTPR PQPGNDKPRL FRLVDAEGLI NRMGFNNLGV
DNLVENVKKA HYDGVLGINI GKNKDTPVEQ GKDDYLICME KIYAYAGYIA INISSPNTPG
LRTLQYGEAL DDLLTAIKNK QNDLQAMHHK YVPIAVKIAP DLSEEELIQV ADSLVRHNID
GVIATNTTLD RSLVQGMKNC DQTGGLSGRP LQLKSTEIIR RLSLELNGRL PIIGVGGIDS
VIAAREKIAA GASLVQIYSG FIFKGPPLIK EIVTHI
//