ID A0A245ZLC2_9SPHN Unreviewed; 368 AA.
AC A0A245ZLC2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Name=flhA_2 {ECO:0000313|EMBL:OWK30537.1};
GN ORFNames=SPMU_15240 {ECO:0000313|EMBL:OWK30537.1};
OS Sphingomonas mucosissima.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=370959 {ECO:0000313|EMBL:OWK30537.1, ECO:0000313|Proteomes:UP000197783};
RN [1] {ECO:0000313|EMBL:OWK30537.1, ECO:0000313|Proteomes:UP000197783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17494 {ECO:0000313|EMBL:OWK30537.1,
RC ECO:0000313|Proteomes:UP000197783};
RA Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Sphingomonas mucosissima DSM 17494.";
RL Submitted (MAR-2017) 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}.
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:OWK30537.1}.
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DR EMBL; NBBJ01000002; OWK30537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A245ZLC2; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000197783; 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}; Zinc {ECO:0000256|RuleBase:RU362016}.
FT DOMAIN 28..112
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..328
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 368 AA; 39317 MW; 40782D85A189F45B CRC64;
MKTRAAVAFE AKKPLEIVEL DLEGPKAGEV LVEIMATGIC HTDAYTLDGL DSEGIFPSIL
GHEGCGIVRE VGAGVTSVAP DDHVIPLYTP ECRQCKSCLS QKTNLCTAIR ATQGKGVMPD
GTSRFSYKGQ QIFHYMGCST FSNFTVLPEI ALAKIRTDAP CDTSCYIGCG VTTGVGAVVH
TAKVEPGATV IVFGLGGIGL NVIQGAKFAG AARIVGVDIN PDREEWGRKF GMTDFVNPKD
VGDIVQHLVA MTDGGGDYTF DCTGNTVVMR QALESAHRGW GESIVIGVAE AGKEIATRPF
QLVTGRVWKG TAFGGARGRT DVPKIVDWYM NGLIQIDPMI THRLTLDEIN KGFDLMHAGE
SIRSVVVY
//
