ID A0A0F4R927_9GAMM Unreviewed; 371 AA.
AC A0A0F4R927;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00021865, ECO:0000256|RuleBase:RU362016};
DE EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016};
GN ORFNames=TW85_04540 {ECO:0000313|EMBL:KJZ16124.1};
OS Marinomonas sp. S3726.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ16124.1, ECO:0000313|Proteomes:UP000033747};
RN [1] {ECO:0000313|EMBL:KJZ16124.1, ECO:0000313|Proteomes:UP000033747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3726 {ECO:0000313|EMBL:KJZ16124.1,
RC ECO:0000313|Proteomes:UP000033747};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000256|ARBA:ARBA00001030,
CC ECO:0000256|RuleBase:RU362016};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000256|ARBA:ARBA00001646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000781};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU362016};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000256|ARBA:ARBA00010902,
CC ECO:0000256|RuleBase:RU362016}.
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:KJZ16124.1}.
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DR EMBL; JXYC01000004; KJZ16124.1; -; Genomic_DNA.
DR RefSeq; WP_046015845.1; NZ_JXYC01000004.1.
DR AlphaFoldDB; A0A0F4R927; -.
DR PATRIC; fig|579484.3.peg.934; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000033747; Unassembled WGS sequence.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR CDD; cd08300; alcohol_DH_class_III; 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; IPR014183; ADH_3.
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 NCBIfam; TIGR02818; adh_III_F_hyde; 1.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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|RuleBase:RU362016};
KW NAD {ECO:0000256|RuleBase:RU362016};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362016};
KW Reference proteome {ECO:0000313|Proteomes:UP000033747};
KW Zinc {ECO:0000256|RuleBase:RU362016}.
FT DOMAIN 12..367
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 371 AA; 39381 MW; B82072C8CDEA1B81 CRC64;
MKSRAAIAWQ AGQPLVIDEI DVQGPKAGEV LVRMVATGVC HTDAFTLSGA DPEGIFPSVL
GHEGAGIVEE VGAGVTTLKP GDHVIPLYTA ECGKCKFCLS GKTNLCQAVR ETQGKGLMPD
GTSRFSIGGK TLYHYMGTST FSEYSVVPEI SLAKIHVDAP LEKVCLLGCG ITTGIGAVLN
TAKVEPGSTV AVFGLGGIGL SVIQGARMAN ASRIIAIDTN ESKFEMAKQF GATDFVNPKD
FSDPIQQVIV DMTDGGVDYS FECIGNVQVM RQALECCHKG WGESIVIGVA GAGEEISTRP
FQLVTGRVWK GSAFGGVKGR SQLPGYVEQY MNGEIEIDPF ITHTMGLEDI NHAFDLMHEG
KSIRSVILFD K
//
