ID J6LL72_9RHOB Unreviewed; 352 AA.
AC J6LL72;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EJW13423.1};
GN ORFNames=A33M_3843 {ECO:0000313|EMBL:EJW13423.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW13423.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW13423.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW13423.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:EJW13423.1}.
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DR EMBL; AKZI01000008; EJW13423.1; -; Genomic_DNA.
DR RefSeq; WP_008382701.1; NZ_AKZI01000008.1.
DR AlphaFoldDB; J6LL72; -.
DR STRING; 1187851.A33M_3843; -.
DR PATRIC; fig|1187851.3.peg.357; -.
DR eggNOG; COG1064; Bacteria.
DR OrthoDB; 5295340at2; -.
DR Proteomes; UP000002930; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002930};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 352 AA; 37370 MW; 3863FA89F92AF4BE CRC64;
MFTCTGYAAE TATAPLAPFT FQRRDPGPTD VVIEILYCGV CHSDIHTVRN EWGGTLYPSL
PGHEIVGKVT AVGADVTKFA VGDVAAVGCM VDSCGTCAAC REGLEQYCEP GFVGTYNGRD
DAAVGGHTFG GYSSHIVVTQ DFVLKVPKNL DLAAAAPLLC AGITTYSPLR HWKAGPGKKV
GIVGLGGLGH MGVKLAHAMG AHVVLFTTSK SKVADGKRLG ADEVVLSTDP EQMKAHAESF
DLIVDAVAAP HDINAYLGLV KREGTLVQVG APDKPLAVDV FSVIWRRRNF AGSLIGGIAE
TQEMLDFCGE HGITSDIEMI PIDKINEAYE RMLKSDVKYR FVIDMASLKK AA
//