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Database: UniProt
Entry: A0A0H4VE04_9SPHN
LinkDB: A0A0H4VE04_9SPHN
Original site: A0A0H4VE04_9SPHN 
ID   A0A0H4VE04_9SPHN        Unreviewed;       400 AA.
AC   A0A0H4VE04;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 2.
DT   27-MAR-2024, entry version 27.
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=CP97_03610 {ECO:0000313|EMBL:AKQ41324.2};
OS   Aurantiacibacter atlanticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=1648404 {ECO:0000313|EMBL:AKQ41324.2, ECO:0000313|Proteomes:UP000059113};
RN   [1] {ECO:0000313|EMBL:AKQ41324.2, ECO:0000313|Proteomes:UP000059113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RX   PubMed=26220886; DOI=10.1099/ijsem.0.000481;
RA   Zhuang L., Liu Y., Wang L., Wang W., Shao Z.;
RT   "Erythrobacter atlanticus sp. nov., a bacterium from ocean sediment able to
RT   degrade polycyclic aromatic hydrocarbons.";
RL   Int. J. Syst. Evol. Microbiol. 65:3714-3719(2015).
RN   [2] {ECO:0000313|Proteomes:UP000059113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The complete genome sequence of Erythrobacter sp. s21-N3.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011310; AKQ41324.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H4VE04; -.
DR   STRING; 1648404.CP97_03610; -.
DR   KEGG; ery:CP97_03610; -.
DR   Proteomes; UP000059113; 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:UP000059113};
KW   Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          44..398
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   400 AA;  42637 MW;  7DEC7734FB33D549 CRC64;
     MPRSAHQSPQ RENNADSCQA GVAAPIRPQG SHMKTRAAVA FEAKQPLEIV ELDLEGPRAG
     EVLIEIMATG ICHTDAYTLD GLDSEGLFPS VLGHEGAGIV REVGAGVTSV VPGDHVIPLY
     TPECRQCKMC LSGKTNLCSA IRETQGKGLM PDGTSRFSYK GQTIHHYMGC STFSNFTVLP
     EIAVAKIRTD APFETSCYIG CGVTTGVGAV VNTAQVKPGD NVVVFGLGGI GLNVLQGAKM
     AGADRIVGVD LNPAKKEWGE KFGMTDFVNP KETSDVVAHI VEMLDGGADY SFDCTGSTEV
     MRQALECCHK GWGTSIIIGV AEAGKEIATR PFQLVTGRNW RGTAFGGAKG RTDVPKIVDW
     YMNGKIAIDP MITHTLTLDE INKGFDLMHS GESIRSVVVY
//
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