ID F7XC16_SINMM Unreviewed; 343 AA.
AC F7XC16;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=IdnD L-idonate 5-dehydrogenase {ECO:0000313|EMBL:AEH82603.1};
GN Name=idnD {ECO:0000313|EMBL:AEH82603.1};
GN OrderedLocusNames=SM11_pC1530 {ECO:0000313|EMBL:AEH82603.1};
OS Sinorhizobium meliloti (strain SM11).
OG Plasmid pSmeSM11c {ECO:0000313|EMBL:AEH82603.1,
OG ECO:0000313|Proteomes:UP000009045}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH82603.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH82603.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH82603.1,
RC ECO:0000313|Proteomes:UP000009045};
RC PLASMID=pSmeSM11c {ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(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; CP001831; AEH82603.1; -; Genomic_DNA.
DR RefSeq; WP_010967263.1; NZ_JAJJBH010000005.1.
DR AlphaFoldDB; F7XC16; -.
DR GeneID; 61599104; -.
DR KEGG; smx:SM11_pC1530; -.
DR PATRIC; fig|707241.3.peg.5448; -.
DR HOGENOM; CLU_026673_11_5_5; -.
DR OMA; FILGHEC; -.
DR Proteomes; UP000009045; Plasmid pSmeSM11c.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
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 Plasmid {ECO:0000313|EMBL:AEH82603.1};
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 343 AA; 36112 MW; 863C2F4464322616 CRC64;
MKAIVIHTAK DLRVEECAVE KPGPGEVEIR LAAGGICGSD LHYYNHGGFG TVRLKEPMIL
GHEVSGHVAA LGEGVSDLAI GDLVAVSPSR PCGACDYCLK GLPNHCFHMR FYGSAMPFPH
IQGAFRERLV AKASQCVKAE GLSAGEAAMA EPLSVTLHAT RRAGEMLGKR VLVTGCGPIG
TLSILAARRA GAAEIVAADL SERALGFARA VGADRTVNLS EDRDGLVPFS ENKGTFDVLY
ECSGAQPALV AGIQALRPRG VIVQLGLGGD MALPMMAITA KELDLRGSFR FHEEFATAVK
LMQGGLIDVK PLITHTLPLG EALKAFEIAS DKGQSMKTQI AFA
//