ID A0A3A5JDY5_9GAMM Unreviewed; 369 AA.
AC A0A3A5JDY5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|RuleBase:RU362016};
DE EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016};
GN ORFNames=D3260_11550 {ECO:0000313|EMBL:RJS92549.1};
OS Salinisphaera sp. Q1T1-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=2321229 {ECO:0000313|EMBL:RJS92549.1, ECO:0000313|Proteomes:UP000269039};
RN [1] {ECO:0000313|EMBL:RJS92549.1, ECO:0000313|Proteomes:UP000269039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1T1-3 {ECO:0000313|EMBL:RJS92549.1,
RC ECO:0000313|Proteomes:UP000269039};
RA Zayas Rivera J., Montalvo Rodriguez R.;
RT "Draft Genome of Salinisphaera endophytica, a Novel Species of the
RT Salinisphaera Genus Isolated as an Endophyte of Avicennia germinans, at the
RT Solar Salterns of Cabo Rojo.";
RL Submitted (SEP-2018) 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 -!- 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:RJS92549.1}.
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DR EMBL; QZWD01000011; RJS92549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5JDY5; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000269039; Unassembled WGS sequence.
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 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 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:UP000269039};
KW Zinc {ECO:0000256|RuleBase:RU362016}.
FT DOMAIN 28..154
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..320
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 369 AA; 39233 MW; 428CDE185B41C31D CRC64;
MKSRAAIAWE AGQPLSVEEI DVEGPKAGEV LVRIVATGVC HTDAFTLSGA DPEGFFPRIL
GHEGGGIVED VGQGVTSLAP GDHVIPLYTA ECGECKFCKS NKTNLCGSVR ETQGQGLMPD
GTSRFSQNGK SLYHYMGTST FSEYTVVPEV SLAKISPEAP LDKVCLLGCG ITTGIGAVFN
TAKVQAGDNV AVFGLGAIGL SVIQGAKMAG ANRIIAIDLN PNKFEFARQL GATECVNPND
YDDPIQNVIV DMTDGGVEHS FECIGNTNVM RSALECCHKG WGESTIIGVA GAGETIETRP
FQLVTGRVWR GSAFGGVKGR TQLPDYVGRY MAGEINIDDF VTHDLPFEQI NEAFDLLHEG
KAIRSVLHF
//
