ID A0A0N9UEH6_SPHMC Unreviewed; 370 AA.
AC A0A0N9UEH6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00021865, ECO:0000256|RuleBase:RU362016};
DE EC=1.1.1.284 {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
GN ORFNames=AN936_16095 {ECO:0000313|EMBL:ALH81820.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH81820.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH81820.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH81820.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(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 -!- 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}.
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DR EMBL; CP012700; ALH81820.1; -; Genomic_DNA.
DR RefSeq; WP_054588966.1; NZ_CP012700.1.
DR AlphaFoldDB; A0A0N9UEH6; -.
DR KEGG; smag:AN936_16095; -.
DR PATRIC; fig|33050.5.peg.3337; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000058074; Chromosome.
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:UP000058074};
KW Zinc {ECO:0000256|RuleBase:RU362016}.
FT DOMAIN 13..368
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 370 AA; 39411 MW; C079237C85BB4DE5 CRC64;
MKTRAAVAFE AKKPLEIVEL DLEGPKAGEV LVEIMATGIC HTDAYTLDGF DSEGIFPSVL
GHEGAGVVRE VGAGVTSVKP GDHVIPLYTP ECRQCKSCLS GKTNLCTAIR ATQGKGLMPD
GTTRFSYNGQ PIFHYMGCST FSNFTVLPEI AVAKIREDAP FQSSCYIGCG VTTGVGAVIN
TAKVQVGDNV VVFGLGGIGL NVIQGARLAG ADKIIGVDIN PDREEWGRKF GMTDFLNSKG
MSREDVVAMI VAMTDGGADY TFDATGNTEV MRIALEACHR GWGTSIIIGV AEAGKEIATR
PFQLVTGRNW RGTAFGGAKG RTDVPKIVDM YMTGKIEIDP MITHVMGLEE INKGFDLMHA
GESIRSVVVF
//
