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Database: UniProt
Entry: A0A037ZMY8_9RHOB
LinkDB: A0A037ZMY8_9RHOB
Original site: A0A037ZMY8_9RHOB 
ID   A0A037ZMY8_9RHOB        Unreviewed;       370 AA.
AC   A0A037ZMY8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=ACMU_00505 {ECO:0000313|EMBL:KAJ57005.1};
OS   Actibacterium mucosum KCTC 23349.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Actibacterium.
OX   NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ57005.1, ECO:0000313|Proteomes:UP000026249};
RN   [1] {ECO:0000313|EMBL:KAJ57005.1, ECO:0000313|Proteomes:UP000026249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ57005.1,
RC   ECO:0000313|Proteomes:UP000026249};
RA   Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT   "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT   Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT   Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL   Submitted (MAR-2014) 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:KAJ57005.1}.
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DR   EMBL; JFKE01000001; KAJ57005.1; -; Genomic_DNA.
DR   RefSeq; WP_035255181.1; NZ_JFKE01000001.1.
DR   AlphaFoldDB; A0A037ZMY8; -.
DR   STRING; 1454373.ACMU_00505; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000026249; 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:UP000026249};
KW   Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          28..113
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          198..330
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   370 AA;  39482 MW;  BA3272F71DB71545 CRC64;
     MRTKAAVALE AGKPMEIMEV NLDGPKAGEV LIEIKATGIC HTDEFTLSGA DPEGIFPTIL
     GHEGAGVVLE VGEGVTSLQP GDHVIPLYTP ECRECEYCLN PKTNLCQSIR STQGQGLMPD
     GTTRFSMLDG TPIYHYMGCS TFANHTVMPE IALAKVRKDA PFDKICYIGC GVTTGIGAVI
     NTAKVEIGSR CVVFGLGGIG LNVIQGLRMA GADQIVGVDL NPAKEDMARY FGMTDYVNPE
     DVKGDMVAHL VELTGGGADY TFDATGNVDV MRTALEAAHK GWGESVIIGV APAGAEISTR
     PFQLVTGRVW RGTAFGGAKG RTDVPKIVDW YMDGKIEIDP MITHVLNLEE INKGFDLMHA
     GESIRAVVVY
//
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