ID J3DLQ8_9BURK Unreviewed; 339 AA.
AC J3DLQ8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=PMI16_00037 {ECO:0000313|EMBL:EJL94591.1};
OS Herbaspirillum sp. CF444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL94591.1, ECO:0000313|Proteomes:UP000007296};
RN [1] {ECO:0000313|EMBL:EJL94591.1, ECO:0000313|Proteomes:UP000007296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF444 {ECO:0000313|EMBL:EJL94591.1,
RC ECO:0000313|Proteomes:UP000007296};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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:EJL94591.1}.
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DR EMBL; AKJW01000004; EJL94591.1; -; Genomic_DNA.
DR RefSeq; WP_007875190.1; NZ_AKJW01000004.1.
DR AlphaFoldDB; J3DLQ8; -.
DR STRING; 1144319.PMI16_00037; -.
DR PATRIC; fig|1144319.3.peg.31; -.
DR eggNOG; COG0604; Bacteria.
DR OrthoDB; 9785812at2; -.
DR Proteomes; UP000007296; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR InterPro; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02817; adh_fam_1; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 13..336
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 339 AA; 36129 MW; DC58133E10C2B290 CRC64;
MKAVAVKRYL PIDNPESLLD VDLPRPTPQG RDLLVAVKAI AVNPVDTKVR APKDTVEDTP
RVLGWDAAGI VEAVGADVSG FKVGDKVFYA GDITRPGSNS EFQLVDERIV GHAPASLAME
EAAALPLTAI TAWEALFERL RVSRKAASGK ASSILIIGGA GGVGSIAIQL AAKVVGLNVI
ATASRPESEK WVRELGAQQV INHFGDMPAQ LKALGVEQVE HVLILNDTDK HFPAAAQIVA
PQGTIATIVE NNGPLDVSLL KAKSAGFFWE FMFTRSMFQT PDMAEQGKLL DEISHLIDQG
VIKTTVSKVL SPINAANLRQ AHADLEGGRV IGKIVLKDF
//
