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6PGL_THEMA
ID   6PGL_THEMA              Reviewed;         220 AA.
AC   Q9X0N8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=6-phosphogluconolactonase;
DE            Short=6PGL;
DE            EC=3.1.1.31;
GN   Name=pgl; Synonyms=devB; OrderedLocusNames=TM_1154;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC         + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       2/3.
CC   -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC       isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}.
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DR   EMBL; AE000512; AAD36230.1; -; Genomic_DNA.
DR   PIR; F72289; F72289.
DR   RefSeq; NP_228960.1; NC_000853.1.
DR   RefSeq; WP_008195599.1; NZ_CP011107.1.
DR   PDB; 1PBT; X-ray; 1.70 A; A=1-220.
DR   PDB; 1VL1; X-ray; 1.55 A; A=1-220.
DR   PDBsum; 1PBT; -.
DR   PDBsum; 1VL1; -.
DR   AlphaFoldDB; Q9X0N8; -.
DR   SMR; Q9X0N8; -.
DR   STRING; 243274.THEMA_08570; -.
DR   DrugBank; DB04272; Citric acid.
DR   DrugBank; DB01942; Formic acid.
DR   EnsemblBacteria; AAD36230; AAD36230; TM_1154.
DR   KEGG; tma:TM1154; -.
DR   eggNOG; COG0363; Bacteria.
DR   InParanoid; Q9X0N8; -.
DR   OMA; YQLFEFE; -.
DR   OrthoDB; 1828393at2; -.
DR   UniPathway; UPA00115; UER00409.
DR   EvolutionaryTrace; Q9X0N8; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR   CDD; cd01400; 6PGL; 1.
DR   InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR   InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR039104; PGLS.
DR   PANTHER; PTHR11054; PTHR11054; 1.
DR   Pfam; PF01182; Glucosamine_iso; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR01198; pgl; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..220
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_0000090108"
FT   STRAND          4..11
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           13..31
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           45..52
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          62..72
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           80..87
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   TURN            88..91
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           108..122
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          151..156
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          167..170
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          179..187
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           188..198
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:1VL1"
FT   STRAND          211..219
FT                   /evidence="ECO:0007829|PDB:1VL1"
SQ   SEQUENCE   220 AA;  25325 MW;  9B0FD07EE01E60C3 CRC64;
     MEKTVIYLLE DGYVDFVVEK IRTKMEKLLE EKDKIFVVLA GGRTPLPVYE KLAEQKFPWN
     RIHFFLSDER YVPLDSDQSN FRNINEVLFS RAKIPSGNVH YVDTSLPIEK ACEKYEREIR
     SATDQFDLAI LGMGPDGHVA SIFDLETGNK DNLVTFTDPS GDPKVPRVTL TFRALNTSLY
     VLFLIRGKEK INRLTEILKD TPLPAYFVRG KEKTVWFVGK
 
 
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