ID Q3ACJ3_CARHZ Unreviewed; 345 AA.
AC Q3ACJ3;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:ABB14675.1};
DE EC=1.1.1.14 {ECO:0000313|EMBL:ABB14675.1};
GN Name=gutB {ECO:0000313|EMBL:ABB14675.1};
GN OrderedLocusNames=CHY_1307 {ECO:0000313|EMBL:ABB14675.1};
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194 {ECO:0000313|EMBL:ABB14675.1, ECO:0000313|Proteomes:UP000002706};
RN [1] {ECO:0000313|EMBL:ABB14675.1, ECO:0000313|Proteomes:UP000002706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901
RC {ECO:0000313|Proteomes:UP000002706};
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C.,
RA Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B.,
RA Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP000141; ABB14675.1; -; Genomic_DNA.
DR RefSeq; WP_011344217.1; NC_007503.1.
DR AlphaFoldDB; Q3ACJ3; -.
DR STRING; 246194.CHY_1307; -.
DR KEGG; chy:CHY_1307; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_5_9; -.
DR InParanoid; Q3ACJ3; -.
DR OrthoDB; 9777057at2; -.
DR Proteomes; UP000002706; Chromosome.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABB14675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..340
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 345 AA; 37205 MW; 20EB69E1ADA23B68 CRC64;
MKAAVLMEPK KIIFKEVPVP ELEKGKVLIK VEAVGICGSD MHLYLDGHIG ATVLDKPLVL
GHEIVGTVIE VGEGVNRELL GQRVIVDPGE NCGQCEHCRT GAYNLCSFSK FKGIPPVDGG
MAEYITALAT HVIPLPENLD SPTATLLEPF SVGLQAVDVA DFRAGAKIAV LGGGPVGVLT
AIAAKIRGCG DLWLTELYER RIEIARKLGI EKVINVAQED PLKTIMEVTK KSGVDVVFET
TGNPKAVEQA LQIVKRGGTV VFLGIGAGKV PINIDQVTRT GLKLLGSFRY QYHFAGAVAL
VKKHNLDFSP LVTNIYDFVD IPKALEEVST YKDRIMKGVI VFPQK
//