ID B3PF26_CELJU Unreviewed; 369 AA.
AC B3PF26;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
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:ACE85528.1};
GN OrderedLocusNames=CJA_3340 {ECO:0000313|EMBL:ACE85528.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE85528.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE85528.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85528.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE85528.1; -; Genomic_DNA.
DR RefSeq; WP_012488916.1; NC_010995.1.
DR AlphaFoldDB; B3PF26; -.
DR STRING; 498211.CJA_3340; -.
DR KEGG; cja:CJA_3340; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_0_6; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:RHEA.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW Zinc {ECO:0000256|RuleBase:RU362016}.
FT DOMAIN 12..367
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 369 AA; 38955 MW; 7CE8940ABE3F323C CRC64;
MKSRAAIALA PGKPLELVDI DVEGPKAGEV LVRIVATSVC HTDAYTLSGA DPEGVFPAVL
GHEGAGIVEA VGPGVTSLAV GDHVIPLYTA ECGKCKFCLS GKTNLCGAVR ATQGKGLMPD
GTTRFSLDGK PLYHYMGTST FSEYTVLPEV SLARVSKEAP LDKICLLGCG VTTGIGAVIN
TAKVTPGSTV AVFGLGAIGL AVIQGAQMVK AARIIAIDVN PDKFELARQF GATDFVNPKD
HSAPIQQVIV DMTDGGVDYS FECIGNVNVM RSALECCHKG WGESIIIGVA GAGQEISTRP
FQLVTGRVWR GSAFGGVKGR SQLPGYVERY MNGEIKIDEF ITHDMPFDQI NQAFDLLHEG
KSIRTVLHY
//