ID A0A0P1HHU9_9RHOB Unreviewed; 364 AA.
AC A0A0P1HHU9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=S-(Hydroxymethyl)mycothiol dehydrogenase {ECO:0000313|EMBL:CUH89549.1};
DE EC=1.1.1.306 {ECO:0000313|EMBL:CUH89549.1};
GN ORFNames=PH5382_03496 {ECO:0000313|EMBL:CUH89549.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH89549.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH89549.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH89549.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CYSG01000022; CUH89549.1; -; Genomic_DNA.
DR RefSeq; WP_058335637.1; NZ_CYSG01000022.1.
DR AlphaFoldDB; A0A0P1HHU9; -.
DR STRING; 1712645.PH5382_03496; -.
DR OrthoDB; 9770544at2; -.
DR Proteomes; UP000050782; Unassembled WGS sequence.
DR GO; GO:0050607; F:mycothiol-dependent formaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CUH89549.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..360
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 364 AA; 37831 MW; 3DBE010F528766B7 CRC64;
MQTIKAAVCH AFGEPLVIEE IQIEDPRMGE VEVTLDAVAI CHSDISFAEG AWGGFLPSVY
GHEAAGVVTQ VGEGVSGFAE GDSVVVTLIR SCGSCPSCAS GKPTICETPY DAVKSGPLKT
ADGAPLMQAM ACGAFAEKVV VDQRQIVKIP ETLSKEAAAL ISCGVITGVG AAVNAAGLRA
GQDVVVIGAG GVGLNAIQGA RIAGARRIVA IDMTEEKLEI AKEFGATDGV LGTLKSPWKA
AFKALGGKGA DVVLVTVGAI PAYEQALRYL GYGGKAVMIG MPHSGQKATY EPVIMAAVGQ
GMIGSKMGDV VIQRDIPWMV DLYEQGRLKL DELISGRWEL EQINEAIADT KTGSAKRNVI
LFNR
//