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Database: UniProt
Entry: J4J6H0_9BURK
LinkDB: J4J6H0_9BURK
Original site: J4J6H0_9BURK 
ID   J4J6H0_9BURK            Unreviewed;       369 AA.
AC   J4J6H0; A0A366G4E6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=N5K24_15430 {ECO:0000313|EMBL:MDH2051795.1};
OS   Achromobacter marplatensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=470868 {ECO:0000313|EMBL:MDH2051795.1, ECO:0000313|Proteomes:UP001161276};
RN   [1] {ECO:0000313|EMBL:MDH2051795.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GD03676 {ECO:0000313|EMBL:MDH2051795.1};
RA   Diorio-Toth L.;
RT   "Intensive care unit water sources are persistently colonized with multi-
RT   drug resistant bacteria and are the site of extensive horizontal gene
RT   transfer of antibiotic resistance genes.";
RL   Submitted (SEP-2022) 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:MDH2051795.1}.
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DR   EMBL; JAOCKG010000005; MDH2051795.1; -; Genomic_DNA.
DR   RefSeq; WP_006226777.1; NZ_QNRM01000003.1.
DR   Proteomes; UP001161276; 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   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}; Zinc {ECO:0000256|RuleBase:RU362016}.
SQ   SEQUENCE   369 AA;  39034 MW;  3FEC51A0D961A952 CRC64;
     MKSRAAVAFG PGKPLEIVEI DVAPPQRGEV LVQITHTGVC HTDAFTLSGD DPEGLFPAVL
     GHEGAGIVVE VGEGVTSLKP GDHVIPLYTA ECRECKFCLS GKTNLCQKVR ATQGKGVMPD
     GTSRFSYEGK PLYHYMGCST FSEYSVVNEI SLAKINPAAP HEKVCLLGCG VTTGLGAVHN
     TAKVKEGDTV AVFGLGGIGL AVIQGAVQAK AGRIIAVDTN PNKFVLASAM GATDCINPKD
     HDKPIQDVIV ELTDGGVDFS FECIGNVHVM RAALECCHKG WGESIIIGVA GAGQEISTRP
     FQLVTGRVWR GSAFGGVKGR TQLPGMVEDA MSGKIDLDPF VTHTLPLERI NEAFDLMHEG
     KSIRTVIHF
//
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