ID A0A089HJ22_PAEDU Unreviewed; 347 AA.
AC A0A089HJ22;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=PDUR_03070 {ECO:0000313|EMBL:AIQ11097.1};
OS Paenibacillus durus (Paenibacillus azotofixans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44251 {ECO:0000313|EMBL:AIQ11097.1, ECO:0000313|Proteomes:UP000029409};
RN [1] {ECO:0000313|EMBL:AIQ11097.1, ECO:0000313|Proteomes:UP000029409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1735 {ECO:0000313|EMBL:AIQ11097.1,
RC ECO:0000313|Proteomes:UP000029409};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009288; AIQ11097.1; -; Genomic_DNA.
DR RefSeq; WP_042205028.1; NZ_CP009288.1.
DR AlphaFoldDB; A0A089HJ22; -.
DR STRING; 44251.PDUR_03070; -.
DR KEGG; pdu:PDUR_03070; -.
DR eggNOG; COG0604; Bacteria.
DR OrthoDB; 9792162at2; -.
DR Proteomes; UP000029409; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; 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 InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 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:UP000029409};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 19..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 347 AA; 38102 MW; BE1A4D7F3CB1787F CRC64;
MSNLQKMKAV GSYRYLPLTD PESLVDLYIE KPVPTGRDLL VKVKAISVNP ADLDIREKNN
YEAESPKILG WDVSGIVEQV GPECQLFKPG DEVFYAGSVT RSGGNSEFHL VDERIAGYKP
KSLDFAQAAA LPLTSLTAWE GLFDRLGISH SSEENESILI IGAAGGVGSI AVQLAKLAGL
TVIGTASRPE SVQWAKDHGA DFTINHNSPF APQLKEIGFE TVDYIFCLND TVQHFANMTE
VIAPQGKICS IVPVAKASQA GSLDMDLLFY KSVTFVWELM FTRAMFQTKD MSKQHDILKQ
LAELIDNGKL KTTLAERLEP INAVNLRLAH EKMETGRSIG KIVLENF
//
