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GDH_AGRFC
ID   GDH_AGRFC               Reviewed;         256 AA.
AC   A9CES4;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Galactitol 2-dehydrogenase {ECO:0000305};
DE            Short=GDH {ECO:0000305};
DE            EC=1.1.1.16 {ECO:0000269|PubMed:26472925};
DE   AltName: Full=Sorbitol dehydrogenase {ECO:0000303|PubMed:26472925};
DE            Short=SorbD {ECO:0000303|PubMed:26472925};
DE            EC=1.1.1.- {ECO:0000269|PubMed:26472925};
GN   OrderedLocusNames=Atu3164 {ECO:0000312|EMBL:AAK90222.2};
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=26472925; DOI=10.1074/jbc.m115.686857;
RA   Wichelecki D.J., Vetting M.W., Chou L., Al-Obaidi N., Bouvier J.T.,
RA   Almo S.C., Gerlt J.A.;
RT   "ATP-binding cassette (ABC) transport system solute-binding protein-guided
RT   identification of novel D-altritol and galactitol catabolic pathways in
RT   Agrobacterium tumefaciens C58.";
RL   J. Biol. Chem. 290:28963-28976(2015).
CC   -!- FUNCTION: Involved in galactitol catabolism. Catalyzes the oxidation of
CC       galactitol to D-tagatose. Can also catalyze the oxidation of D-sorbitol
CC       to D-fructose. {ECO:0000269|PubMed:26472925}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=galactitol + NAD(+) = H(+) + keto-D-tagatose + NADH;
CC         Xref=Rhea:RHEA:20685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16813,
CC         ChEBI:CHEBI:47693, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.16;
CC         Evidence={ECO:0000269|PubMed:26472925};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+);
CC         Xref=Rhea:RHEA:33031, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924,
CC         ChEBI:CHEBI:48095, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000269|PubMed:26472925};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.0 mM for galactitol {ECO:0000269|PubMed:26472925};
CC         KM=1.9 mM for D-sorbitol {ECO:0000269|PubMed:26472925};
CC         Note=kcat is 3.5 sec(-1) with galactitol as substrate. kcat is 4.4
CC         sec(-1) with D-sorbitol as substrate. {ECO:0000269|PubMed:26472925};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:26472925}.
CC   -!- INDUCTION: Up-regulated by growth on D-altritol or galactitol.
CC       {ECO:0000269|PubMed:26472925}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant cannot grow on D-galactitol. Does
CC       not exhibit a growth defect when grown on D-altritol.
CC       {ECO:0000269|PubMed:26472925}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AE007870; AAK90222.2; -; Genomic_DNA.
DR   RefSeq; NP_357437.2; NC_003063.2.
DR   RefSeq; WP_010972809.1; NC_003063.2.
DR   AlphaFoldDB; A9CES4; -.
DR   SMR; A9CES4; -.
DR   STRING; 176299.Atu3164; -.
DR   EnsemblBacteria; AAK90222; AAK90222; Atu3164.
DR   GeneID; 66223482; -.
DR   KEGG; atu:Atu3164; -.
DR   PATRIC; fig|176299.10.peg.3009; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_0_5; -.
DR   OMA; ITGGRNW; -.
DR   PhylomeDB; A9CES4; -.
DR   BioCyc; MetaCyc:MON-20146; -.
DR   Proteomes; UP000000813; Chromosome linear.
DR   GO; GO:0047713; F:galactitol 2-dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0019402; P:galactitol metabolic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..256
FT                   /note="Galactitol 2-dehydrogenase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002736555"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q48436"
FT   BINDING         15..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         59..60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         86
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
SQ   SEQUENCE   256 AA;  26712 MW;  5B3602E2EAE3C999 CRC64;
     MRLNNKVALI TGAARGIGLG FAQAFAAEGA KVIIADIDIA RATTSAAAIG PAAKAVKLDV
     TDLAQIDAVV KAVDEEFGGI DILVNNAAIF DMAPINGITE ESYERVFDIN LKGPMFMMKA
     VSNVMIARAR GGKIINMASQ AGRRGEALVT LYCASKAAII SATQSAALAL VKHGINVNAI
     APGVVDGEHW EVVDAHFAKW EGLKPGEKKA AVAKSVPIGR FATPDDIKGL AVFLASADSD
     YILAQTYNVD GGNWMS
 
 
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