ID A0A411HH55_9GAMM Unreviewed; 338 AA.
AC A0A411HH55;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=ELE36_05325 {ECO:0000313|EMBL:QBB69835.1};
OS Pseudolysobacter antarcticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudolysobacter.
OX NCBI_TaxID=2511995 {ECO:0000313|EMBL:QBB69835.1, ECO:0000313|Proteomes:UP000291562};
RN [1] {ECO:0000313|EMBL:QBB69835.1, ECO:0000313|Proteomes:UP000291562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AQ6-296 {ECO:0000313|EMBL:QBB69835.1,
RC ECO:0000313|Proteomes:UP000291562};
RA Wei Z., Peng F.;
RT "Pseudolysobacter antarctica gen. nov., sp. nov., isolated from Fildes
RT Peninsula, Antarctica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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DR EMBL; CP035704; QBB69835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411HH55; -.
DR KEGG; xbc:ELE36_05325; -.
DR OrthoDB; 9785812at2; -.
DR Proteomes; UP000291562; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000291562};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 13..335
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 338 AA; 36559 MW; A4E90B14D83270DC CRC64;
MKAVALTRYL PISDAHSLFD TEIEKPVATA RDLLVRMLAV SVNPVDTKVR SPKDKVESAP
RVLGWDAAGI VEAVGDQVTA FKPGDEVYYA GSIERPGCNS EYQLVDERIV ARKPASLDFA
QAAALPLTAI TAWELMFERM RIGNDGSEHG RNLLVIGGAG GVGSMAIQFG KLAGVTVIAT
ASRADTIAWC RELGADHVID HRQALQPQLD ALGITAIPYI VNFADSAAYW TQMGELIAPQ
GRIGLIVEPS APLPIGDPFK LKSVSIHWEM MFTRAKFQTD DMIEQRHLLA RIAALIDAGK
LRGTMRQNLG SITAENLRKA HALLESGQSI GKIVLAGW
//
