ID   ATRDH_AGRFC             Reviewed;         336 AA.
AC   A9CES3;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=D-altritol 5-dehydrogenase {ECO:0000305};
DE            EC=1.1.1.407 {ECO:0000269|PubMed:26472925};
GN   OrderedLocusNames=Atu3163 {ECO:0000312|EMBL:AAK90223.2};
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 D-altritol catabolism. Catalyzes the oxidation of
CC       D-altritol to D-tagatose. {ECO:0000269|PubMed:26472925}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-altritol + NAD(+) = H(+) + keto-D-tagatose + NADH;
CC         Xref=Rhea:RHEA:51708, ChEBI:CHEBI:15378, ChEBI:CHEBI:47693,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:134311;
CC         EC=1.1.1.407; Evidence={ECO:0000269|PubMed:26472925};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O58389};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O58389};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.4 mM for D-altritol {ECO:0000269|PubMed:26472925};
CC         Note=kcat is 1.9 sec(-1). {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-altritol. Does
CC       not exhibit a growth defect when grown on D-galactitol.
CC       {ECO:0000269|PubMed:26472925}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AE007870; AAK90223.2; -; Genomic_DNA.
DR   RefSeq; NP_357438.2; NC_003063.2.
DR   RefSeq; WP_010972808.1; NC_003063.2.
DR   AlphaFoldDB; A9CES3; -.
DR   SMR; A9CES3; -.
DR   STRING; 176299.Atu3163; -.
DR   EnsemblBacteria; AAK90223; AAK90223; Atu3163.
DR   GeneID; 66223481; -.
DR   KEGG; atu:Atu3163; -.
DR   PATRIC; fig|176299.10.peg.3008; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_5; -.
DR   OMA; PIGCLHV; -.
DR   PhylomeDB; A9CES3; -.
DR   BioCyc; MetaCyc:MON-20147; -.
DR   BRENDA; 1.1.1.407; 14964.
DR   Proteomes; UP000000813; Chromosome linear.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR031640; Glu_dehyd_C.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF16912; Glu_dehyd_C; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..336
FT                   /note="D-altritol 5-dehydrogenase"
FT                   /id="PRO_0000446635"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
SQ   SEQUENCE   336 AA;  35186 MW;  01EEC4959691363D CRC64;
     MHAIQFVEKG RAVLAELPVA DLPPGHALVR VKASGLCHTD IDVLHARYGD GAFPVIPGHE
     YAGEVAAVAS DVTVFKAGDR VVVDPNLPCG TCASCRKGLT NLCSTLKAYG VSHNGGFAEF
     SVVRADHLHG IGSMPYHVAA LAEPLACVVN GMQSAGIGES GVVPENALVF GAGPIGLLLA
     LSLKSRGIAT VTMADINESR LAFAQDLGLQ TAVSGSEALS RQRKEFDFVA DATGIAPVAE
     AMIPLVADGG TALFFGVCAP DARISVAPFE IFRRQLKLVG SHSLNRNIPQ ALAILETDGE
     VMARLVSHRL PLSEMLPFFT KKPSDPATMK VQFAAE