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DGOK_RHIME
ID   DGOK_RHIME              Reviewed;         306 AA.
AC   Q92RN7;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Probable 2-dehydro-3-deoxygalactonokinase DgoK1;
DE            EC=2.7.1.58;
DE   AltName: Full=2-keto-3-deoxy-galactonokinase;
DE   AltName: Full=2-oxo-3-deoxygalactonate kinase;
GN   Name=dgoK1; OrderedLocusNames=R00825; ORFNames=SMc00881;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=1021;
RX   PubMed=22797764; DOI=10.1128/jb.00982-12;
RA   Geddes B.A., Oresnik I.J.;
RT   "Inability to catabolize galactose leads to increased ability to compete
RT   for nodule occupancy in Sinorhizobium meliloti.";
RL   J. Bacteriol. 194:5044-5053(2012).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RG   New York Structural Genomics Research Consortium (NYSGRC);
RT   "Crystal structure of a putative 2-dehydro-3-deoxygalactonokinase protein
RT   from Sinorhizobium meliloti.";
RL   Submitted (JUL-2011) to the PDB data bank.
CC   -!- FUNCTION: Involved in the degradation of galactose via the DeLey-
CC       Doudoroff pathway. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-D-galactonate + ATP = 2-dehydro-3-deoxy-6-
CC         phospho-D-galactonate + ADP + H(+); Xref=Rhea:RHEA:16525,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57989,
CC         ChEBI:CHEBI:58298, ChEBI:CHEBI:456216; EC=2.7.1.58;
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-galactonate degradation; D-
CC       glyceraldehyde 3-phosphate and pyruvate from D-galactonate: step 2/3.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on galactose
CC       as sole carbon source. {ECO:0000269|PubMed:22797764}.
CC   -!- SIMILARITY: Belongs to the DgoK family. {ECO:0000305}.
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DR   EMBL; AL591688; CAC45397.1; -; Genomic_DNA.
DR   RefSeq; NP_384931.1; NC_003047.1.
DR   RefSeq; WP_010968850.1; NC_003047.1.
DR   PDB; 3T69; X-ray; 2.55 A; A/B=1-306.
DR   PDBsum; 3T69; -.
DR   AlphaFoldDB; Q92RN7; -.
DR   SMR; Q92RN7; -.
DR   STRING; 266834.SMc00881; -.
DR   PRIDE; Q92RN7; -.
DR   EnsemblBacteria; CAC45397; CAC45397; SMc00881.
DR   GeneID; 61602291; -.
DR   KEGG; sme:SMc00881; -.
DR   PATRIC; fig|266834.11.peg.2215; -.
DR   eggNOG; COG3734; Bacteria.
DR   HOGENOM; CLU_058005_2_0_5; -.
DR   OMA; HFDTFMT; -.
DR   UniPathway; UPA00081; UER00519.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0008671; F:2-dehydro-3-deoxygalactonokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034194; P:D-galactonate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.420.300; -; 1.
DR   Gene3D; 3.30.420.310; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR007729; DGOK.
DR   InterPro; IPR042257; DGOK_C.
DR   InterPro; IPR042258; DGOK_N.
DR   Pfam; PF05035; DGOK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..306
FT                   /note="Probable 2-dehydro-3-deoxygalactonokinase DgoK1"
FT                   /id="PRO_0000428931"
FT   STRAND          7..12
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          17..22
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          28..35
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           38..44
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           91..94
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          100..104
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          121..125
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           126..134
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          142..146
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          148..157
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          160..167
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           169..179
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           183..186
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           213..227
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           231..251
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          259..264
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           266..278
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   STRAND          282..287
FT                   /evidence="ECO:0007829|PDB:3T69"
FT   HELIX           288..303
FT                   /evidence="ECO:0007829|PDB:3T69"
SQ   SEQUENCE   306 AA;  31733 MW;  ACF24F42B776FA6B CRC64;
     MTTAGYYAAV DWGTSSFRLW IIGEDGAVLA ERRSAEGMTT AAKTGFHTIL DGHLAAVSAP
     AHLPIIICGM AGARQGWKEA GYIETPAALA EIAGRATAIP DVDRDIRILP GLAQRDRRHP
     DVMRGEETQL LGAAAHLGAG SHLVCMPGTH SKWVRLADDR VEGFSTFMTG ELFDTIARHT
     ILSHAVAEAD TFAAGSAAFT DAVSRTRENP ALATNLLFSV RAGQLLHGTA AADARAQLSG
     TLIGLEIAGA LAGSGSVDGV CLVGSGGLGT LYRTALESQG LNVRAVDADE AVRAGLSAAA
     RAIWPL
 
 
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