ID M5EHJ9_9FIRM Unreviewed; 727 AA.
AC M5EHJ9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:CCU80938.1};
DE EC=1.1.1.14 {ECO:0000313|EMBL:CCU80938.1};
GN ORFNames=HSACCH_02440 {ECO:0000313|EMBL:CCU80938.1};
OS Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU80938.1, ECO:0000313|Proteomes:UP000012063};
RN [1] {ECO:0000313|Proteomes:UP000012063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL Genome Announc. 1:217-225(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCU80938.1}.
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DR EMBL; CAUI01000023; CCU80938.1; -; Genomic_DNA.
DR RefSeq; WP_005490252.1; NZ_CAUI01000023.1.
DR AlphaFoldDB; M5EHJ9; -.
DR STRING; 1293054.HSACCH_02440; -.
DR eggNOG; COG0673; Bacteria.
DR eggNOG; COG1063; Bacteria.
DR InParanoid; M5EHJ9; -.
DR OrthoDB; 9815825at2; -.
DR Proteomes; UP000012063; Unassembled WGS sequence.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR CDD; cd08255; 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43350:SF22; D-GULOSIDE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CCU80938.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012063}.
FT DOMAIN 47..363
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 727 AA; 80021 MW; 96C66EB42D2F2C6A CRC64;
MLQVMQNYKG GDLRVEEVPS PVLQPGGVLV KNHNSLISAG TEKSIINLAQ SSIVSKAKQR
PDLVKQVLEK VKQEGLINTF KKVMGKLDSP MSVGYSCAGE VVAVASDVKD LKVGDRVACA
GAGYANHAEM IYAPRNLTAK IPEGVSYEEA SFSTVASIAL QGIRQAEPKL GENVAVIGLG
LIGLLTAEML KANGCNVIGI DVSEFAVSNA KKLGHQNSFL RGKENLKSKV NNLTNGQGVD
SILITASADS NDPVEFAGEI ARDRAKVVAV GMVGLDIPRN LYYEKELDLR LSRSYGPGRY
DTDYEEKGYD YPIGYVRWTE QRNMQAFLNL LADQKIDLDK IITHKFKIEK AKEAYDMILE
NKESYLGVLL EYDTEKSLPA KIQVKENTSR GDKINLAMVG AGNFAKGVLI PNLAKINNIN
FNTLVTATGA SAKNTAKKFD FNYCTTDENE VYKDNEVNTV FITTRHNLHA DSVIKGLENN
KNVYVEKPLG LYEADLENII KAWDKSEGKL MVGFNRRFSP FTKELKEFYQ NRNTPLVMNY
TVNAGYIPGD HWTQDPEIGG GRIKGEVCHF LDLLSYIADS EPVSVYAQPI SANTEHIFND
DNLLVSIYFA DGSVGNITYT ALGDSSYPKE RIEAFADSAA AILDNFNSLT THSNNKSDTS
KKFSQQKGFK EELEAFADSI EKGKESPINF KSLIASSLAT LKIIESMEQG KPVEVNVDQF
INNALDY
//
