ID A0A0R0E577_9GAMM Unreviewed; 369 AA.
AC A0A0R0E577;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00021865, ECO:0000256|RuleBase:RU362016};
DE EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016};
GN Name=adhC {ECO:0000313|EMBL:ALJ27181.1};
GN ORFNames=ABB33_10200 {ECO:0000313|EMBL:KRG85204.1}, AOT14_07450
GN {ECO:0000313|EMBL:ALJ27181.1};
OS Stenotrophomonas acidaminiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=128780 {ECO:0000313|EMBL:KRG85204.1, ECO:0000313|Proteomes:UP000050958};
RN [1] {ECO:0000313|EMBL:ALJ27181.1, ECO:0000313|Proteomes:UP000061010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZAC14D2_NAIMI4_2 {ECO:0000313|EMBL:ALJ27181.1,
RC ECO:0000313|Proteomes:UP000061010};
RX PubMed=26659678;
RA Vinuesa P., Ochoa-Sanchez L.E.;
RT "Complete Genome Sequencing of Stenotrophomonas acidaminiphila
RT ZAC14D2_NAIMI4_2, a Multidrug-Resistant Strain Isolated from Sediments of a
RT Polluted River in Mexico, Uncovers New Antibiotic Resistance Genes and a
RT Novel Class-II Lasso Peptide Biosynthesis Gene Cluster.";
RL Genome Announc. 3:e01433-15(2015).
RN [2] {ECO:0000313|EMBL:KRG85204.1, ECO:0000313|Proteomes:UP000050958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13310 {ECO:0000313|EMBL:KRG85204.1,
RC ECO:0000313|Proteomes:UP000050958};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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 primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001146};
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; CP012900; ALJ27181.1; -; Genomic_DNA.
DR EMBL; LDJO01000026; KRG85204.1; -; Genomic_DNA.
DR RefSeq; WP_054663042.1; NZ_LDJO01000026.1.
DR AlphaFoldDB; A0A0R0E577; -.
DR KEGG; sacz:AOT14_07450; -.
DR PATRIC; fig|128780.6.peg.753; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000050958; Unassembled WGS sequence.
DR Proteomes; UP000061010; Chromosome.
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..367
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 369 AA; 38915 MW; 4A3D1AF17C591C7F CRC64;
MKSRAAVAFG PGQPLQIVEI DVAPPKQGEV LVRITHTGVC HTDAFTLSGD DPEGLFPCVL
GHEGAGIVVE VGEGVTSVKP GDHVIPLYTA ECGQCLFCKS GKTNLCTAVR ATQGKGVMPD
GTSRFSYNGE PIYHYMGCST FSEYTVVAEV SLAKVNPEAN PEHVCLLGCG VTTGIGAVHN
TAKVAEGDSV AVFGLGGIGL AVIQGARQAK AGRIIAIDTN PSKFELARQF GATDCVNPKE
HDAPIQQVIV EMTGWGVDHS FECIGNVNVM RAALECAHRG WGQSVIIGVA GAGQEISTRP
FQLVTGRRWM GTAFGGVKGR SQLPGMVEDA MKGDIELAPF VTHTMGLEQI NDAFDLMHEG
KSIRSVVHF
//
