ID A0A0Q9KJW5_9BACL Unreviewed; 350 AA.
AC A0A0Q9KJW5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=ASG81_16180 {ECO:0000313|EMBL:KRE41806.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE41806.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE41806.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE41806.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KRE41806.1}.
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DR EMBL; LMRV01000048; KRE41806.1; -; Genomic_DNA.
DR RefSeq; WP_056636278.1; NZ_LMRV01000048.1.
DR AlphaFoldDB; A0A0Q9KJW5; -.
DR STRING; 1736388.ASG81_16180; -.
DR OrthoDB; 9792162at2; -.
DR Proteomes; UP000051180; Unassembled WGS sequence.
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; IPR013149; ADH-like_C.
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; 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; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 18..346
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 38466 MW; 2CF26D77EAA3B4BB CRC64;
MSNHQKMKAV GAYRYLPLSD PECLVDLYIE KPIPTGRDLL VKVKAISVNP ADLGVREKNN
YEEESPKILG WDVAGIVDQA GPDCQLFKPG DEIYYAGSVT RPGGNSEFHL VDERIAGNKP
KSLDFAQAAA LPLSSITAWE GLFDRLGISH SVEENINKSL LIIGAAGGVG SIATQLAKLA
GLTVIGTASR PESIQWAKDQ GADITINHNS HFASQLKNSG FETVDYIFCL NDTVQHFANM
VEVIAPQGKI CSIVPADKAS WAGSLDMDML FSKSITFVWE LMFTRSMYQT EDMIKQHDLL
NKLADLIDNG KLKSTLTERI EPINATNLRF VHEKIETGRS IGKIVLENFQ
//
