ID F7ZGN3_ROSLO Unreviewed; 343 AA.
AC F7ZGN3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=L-idonate 5-dehydrogenase IdnD {ECO:0000313|EMBL:AEI92333.1};
DE EC=1.1.1.264 {ECO:0000313|EMBL:AEI92333.1};
GN Name=idnD2 {ECO:0000313|EMBL:AEI92333.1};
GN OrderedLocusNames=RLO149_c003030 {ECO:0000313|EMBL:AEI92333.1};
OS Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS 15278 / OCh 149).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391595 {ECO:0000313|EMBL:AEI92333.1, ECO:0000313|Proteomes:UP000001353};
RN [1] {ECO:0000313|EMBL:AEI92333.1, ECO:0000313|Proteomes:UP000001353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
RC {ECO:0000313|Proteomes:UP000001353};
RX PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA Daniel R., Simon M., Brinkhoff T.;
RT "Comparative genome analysis and genome-guided physiological analysis of
RT Roseobacter litoralis.";
RL BMC Genomics 12:324-324(2011).
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; CP002623; AEI92333.1; -; Genomic_DNA.
DR RefSeq; WP_013960276.1; NC_015730.1.
DR AlphaFoldDB; F7ZGN3; -.
DR STRING; 391595.RLO149_c003030; -.
DR KEGG; rli:RLO149_c003030; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_5_5; -.
DR OMA; PHTDGGF; -.
DR OrthoDB; 9809185at2; -.
DR Proteomes; UP000001353; Chromosome.
DR GO; GO:0050572; F:L-idonate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08232; idonate-5-DH; 1.
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:AEI92333.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..340
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 343 AA; 35532 MW; 42A44B530D435969 CRC64;
MKSLVIHGAH DLRIEEHEPQ TLGAGQVQIA LATGGICGSD LHYYHNGGFG TVRLKEPMVL
GHEVSGHITA LGAAVSGLEV GQLVAVSPSR PCGACCYCAE GMRNQCLNMR FYGSAMPFPH
IQGAFRQVLV ADAAQCAVAD GLSAGEAAMA EPLAVCLHAA RQAGPLLGKR VLVTGCGPIG
LLSILVARRA GATEIVATDL TDFTLRMAAA QGADVTINGA TDPDRLATYQ AGKGTFDVLF
ECTGVAAALA GGIAALRPGG IIVQLGLGGD MTLPVQALTA KELQLRGSFR FHEEFFTGVA
LMQKGLIDVK PLITQTLPLA DAIAAFDLAS DRTQAMKAQI SFA
//