ID G2ZM27_9RALS Unreviewed; 368 AA.
AC G2ZM27;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 Name=adhI {ECO:0000313|EMBL:CCA80130.1};
GN ORFNames=BDB_80520 {ECO:0000313|EMBL:CCA80130.1};
OS blood disease bacterium R229.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=741978 {ECO:0000313|EMBL:CCA80130.1};
RN [1] {ECO:0000313|EMBL:CCA80130.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R229 {ECO:0000313|EMBL:CCA80130.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA80130.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R229 {ECO:0000313|EMBL:CCA80130.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) 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 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}.
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DR EMBL; FR854064; CCA80130.1; -; Genomic_DNA.
DR AlphaFoldDB; G2ZM27; -.
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}.
FT DOMAIN 12..366
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 368 AA; 39377 MW; 982CCB8C1CE8C534 CRC64;
MKTKAAIAWK SGAPLTIEDV DLQGPRAGEV LVEIKATGIC HTDYYTLSGA DPEGIFPAIL
GHEGAGVVLD VGAGVTSLKP GDHVIPLYTP ECRQCKFCLS RKTNLCQAIR ATQGKGLMPD
GSSRFSIDGK PIFHYMGTST FANHIVAPEI ALAKIRPDAP FDKVCYIGCG VTTGVGAVVY
TARVEAGANV VVFGLGGIGL NVIQGAKMVG ADKIIGVDLN PAREAMARKF GMTHFVNPKD
VDNVVDHIIQ LTDGGADYSF ECIGNTQVMR QALECCHKGW GQSIIIGVAE AGAEISTRPF
QLVTGRQWKG SAFGGARGRT DVPKIVDWYM EGKLNIDDLI THTLPLERIN EGFDLMKRGE
SIRSVVLY
//