ID A0A1G5FXA3_9PROT Unreviewed; 372 AA.
AC A0A1G5FXA3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
DE EC=1.1.1.284 {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
GN ORFNames=SAMN05216420_106102 {ECO:0000313|EMBL:SCY43992.1};
OS Nitrosospira sp. Nl5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=200120 {ECO:0000313|EMBL:SCY43992.1, ECO:0000313|Proteomes:UP000198645};
RN [1] {ECO:0000313|Proteomes:UP000198645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nl5 {ECO:0000313|Proteomes:UP000198645};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FMVQ01000006; SCY43992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5FXA3; -.
DR STRING; 200120.SAMN05216420_106102; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000198645; 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:UP000198645};
KW Zinc {ECO:0000256|RuleBase:RU362016}.
FT DOMAIN 31..156
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 200..331
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 372 AA; 39622 MW; 4E931B9B0CEF9185 CRC64;
MELIKTRAAV AWGPGQPLRI EEIDLMPPQK GEVLVRIVAT GVCHTDAFTL SGNDPEGKFP
SILGHEGGGI VEALGEGVNS VSVGDHVIPL YTPECGECKF CRSGKTNLCQ AIRMTQGQGL
MPDGTTRFSK NGKPIYHYMG TSTFSEYTVI PEISLAKISK AAPLEKVCLL GCGVTTGLGA
VANTAKVKAG DTVAVFGLGG IGLAVIVGAT MANAGRIIAI DINPEKFEIA RQLGATDVVN
PKDYSRPIQE VVIEMTGGGV DFSFECIGNV KVMRSALECC HKGWGESVII GVAGAGEEIC
TRPFQLVTGR VWRGSAFGGV KGRTELPGYV QRYLDGEFEL DTFITHTMPL DDINTAFDLM
HEGKSIRTVI HF
//
