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GATZ_ECO57
ID   GATZ_ECO57              Reviewed;         420 AA.
AC   Q8X7H4; Q7ACL2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit GatZ;
GN   Name=gatZ; OrderedLocusNames=Z3258, ECs2898;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RG   New York structural genomix research consortium (NYSGXRC);
RT   "Crystal structure of putative tagatose 6-phosphate kinase.";
RL   Submitted (APR-2006) to the PDB data bank.
CC   -!- FUNCTION: Component of the tagatose-1,6-bisphosphate aldolase GatYZ
CC       that is required for full activity and stability of the Y subunit.
CC       Could have a chaperone-like function for the proper and stable folding
CC       of GatY. When expressed alone, GatZ does not show any aldolase
CC       activity. Is involved in the catabolism of galactitol (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation;
CC       D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-
CC       phosphate: step 2/2.
CC   -!- SUBUNIT: Forms a complex with GatY. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GatZ/KbaZ family. GatZ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG57152.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36321.1; -; Genomic_DNA.
DR   PIR; B90991; B90991.
DR   PIR; D85836; D85836.
DR   RefSeq; NP_310925.1; NC_002695.1.
DR   RefSeq; WP_000853846.1; NZ_SWKA01000005.1.
DR   PDB; 2FIQ; X-ray; 2.25 A; A/B/C/D=1-420.
DR   PDBsum; 2FIQ; -.
DR   AlphaFoldDB; Q8X7H4; -.
DR   SMR; Q8X7H4; -.
DR   STRING; 155864.EDL933_3164; -.
DR   DNASU; 916601; -.
DR   EnsemblBacteria; AAG57152; AAG57152; Z3258.
DR   EnsemblBacteria; BAB36321; BAB36321; ECs_2898.
DR   GeneID; 916601; -.
DR   KEGG; ece:Z3258; -.
DR   KEGG; ecs:ECs_2898; -.
DR   PATRIC; fig|386585.9.peg.3030; -.
DR   eggNOG; COG4573; Bacteria.
DR   HOGENOM; CLU_053334_0_0_6; -.
DR   OMA; AINAVHV; -.
DR   UniPathway; UPA00704; UER00716.
DR   EvolutionaryTrace; Q8X7H4; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019404; P:galactitol catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01296; Tagatose_aldol_GatZ; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012062; GatZ/KbaZ-like.
DR   InterPro; IPR023436; TagBP_ald_GatZ.
DR   Pfam; PF08013; GatZ_KbaZ-like; 1.
DR   PIRSF; PIRSF009264; TagBP_ald_AgaZ; 1.
DR   TIGRFAMs; TIGR02810; agaZ_gatZ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Galactitol metabolism; Reference proteome.
FT   CHAIN           1..420
FT                   /note="D-tagatose-1,6-bisphosphate aldolase subunit GatZ"
FT                   /id="PRO_0000355359"
FT   HELIX           2..9
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           24..33
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   TURN            34..36
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   TURN            55..58
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           61..75
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          82..91
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           99..115
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           138..155
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           158..163
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           190..205
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   TURN            206..208
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           210..214
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          216..220
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           237..240
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           241..247
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          253..257
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           264..272
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   STRAND          275..280
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           282..302
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   TURN            305..307
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           311..321
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           323..325
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   TURN            326..329
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           334..343
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           348..351
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   TURN            352..354
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           356..370
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           376..382
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           384..391
FT                   /evidence="ECO:0007829|PDB:2FIQ"
FT   HELIX           399..418
FT                   /evidence="ECO:0007829|PDB:2FIQ"
SQ   SEQUENCE   420 AA;  47022 MW;  9E765977C05F4B6E CRC64;
     MKTLIARHKA GEHIGICSVC SAHPLVIEAA LAFDRNSTRK VLIEATSNQV NQFGGYTGMT
     PADFREFVFA IADKVGFARE RIILGGDHLG PNCWQQENVD AAMEKSVELV KAYVRAGFSK
     IHLDASMSCA GDPIPLAPET VAERAAVLCF AAESVATDCQ REQLSYVIGT EVPVPGGEAS
     AIQSVHITHV EDAANTLRTH QKAFIARGLT EALTRVIAIV VQPGVEFDHS NIIHYQPQEA
     QALAQWIENT RMVYEAHSTD YQTRTAYWEL VRDHFAILKV GPALTFALRE AIFALAQIEQ
     ELIAPENRSG CLAVIEEVML DEPQYWKKYY RTGFNDSLLD IRYSLSDRIR YYWPHSRIKN
     SVETMMVNLQ GVDIPLGMIS QYLPKQFERI QSGELSAIPH QLIMDKIYDV LRAYRYGCAE
 
 
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