SRLD_ECOLI
ID SRLD_ECOLI Reviewed; 259 AA.
AC P05707;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Sorbitol-6-phosphate 2-dehydrogenase;
DE EC=1.1.1.140 {ECO:0000269|PubMed:6384188};
DE AltName: Full=Glucitol-6-phosphate dehydrogenase;
DE AltName: Full=Ketosephosphate reductase;
GN Name=srlD; Synonyms=gutD; OrderedLocusNames=b2705, JW2674;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3553176; DOI=10.1016/s0021-9258(18)45594-9;
RA Yamada M., Saier M.H. Jr.;
RT "Glucitol-specific enzymes of the phosphotransferase system in Escherichia
RT coli. Nucleotide sequence of the gut operon.";
RL J. Biol. Chem. 262:5455-5463(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-34, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=6384188; DOI=10.1128/jb.159.3.986-990.1984;
RA Novotny M.J., Reizer J., Esch F., Saier M.H. Jr.;
RT "Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-
RT glucitol-6-phosphate dehydrogenase from Escherichia coli.";
RL J. Bacteriol. 159:986-990(1984).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol 6-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19837, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:60084; EC=1.1.1.140;
CC Evidence={ECO:0000269|PubMed:6384188};
CC -!- PATHWAY: Carbohydrate metabolism; D-sorbitol degradation; D-fructose 6-
CC phosphate from D-sorbitol 6-phosphate: step 1/1.
CC {ECO:0000305|PubMed:6384188}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:6384188}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; J02708; AAC13413.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69214.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75747.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16566.1; -; Genomic_DNA.
DR PIR; E65050; DEECSP.
DR RefSeq; NP_417185.1; NC_000913.3.
DR RefSeq; WP_001077358.1; NZ_LN832404.1.
DR AlphaFoldDB; P05707; -.
DR SMR; P05707; -.
DR BioGRID; 4260703; 18.
DR BioGRID; 853206; 2.
DR DIP; DIP-10917N; -.
DR IntAct; P05707; 3.
DR STRING; 511145.b2705; -.
DR jPOST; P05707; -.
DR PaxDb; P05707; -.
DR PRIDE; P05707; -.
DR EnsemblBacteria; AAC75747; AAC75747; b2705.
DR EnsemblBacteria; BAA16566; BAA16566; BAA16566.
DR GeneID; 66673426; -.
DR GeneID; 948937; -.
DR KEGG; ecj:JW2674; -.
DR KEGG; eco:b2705; -.
DR PATRIC; fig|1411691.4.peg.4037; -.
DR EchoBASE; EB0964; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_0_6; -.
DR InParanoid; P05707; -.
DR OMA; QGIHFQN; -.
DR PhylomeDB; P05707; -.
DR BioCyc; EcoCyc:SORB6PDEHYDROG-MON; -.
DR BioCyc; MetaCyc:SORB6PDEHYDROG-MON; -.
DR UniPathway; UPA00812; UER00783.
DR PRO; PR:P05707; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009010; F:sorbitol-6-phosphate 2-dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0006062; P:sorbitol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..259
FT /note="Sorbitol-6-phosphate 2-dehydrogenase"
FT /id="PRO_0000054779"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 4..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 68
FT /note="V -> C (in Ref. 1; AAC13413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 27858 MW; 29C6215F857B5FBC CRC64;
MNQVAVVIGG GQTLGAFLCH GLAAEGYRVA VVDIQSDKAA NVAQEINAEY GESMAYGFGA
DATSEQSVLA LSRGVDEIFG RVDLLVYSAG IAKAAFISDF QLGDFDRSLQ VNLVGYFLCA
REFSRLMIRD GIQGRIIQIN SKSGKVGSKH NSGYSAAKFG GVGLTQSLAL DLAEYGITVH
SLMLGNLLKS PMFQSLLPQY ATKLGIKPDQ VEQYYIDKVP LKRGCDYQDV LNMLLFYASP
KASYCTGQSI NVTGGQVMF
