ID A0A023Y9M0_9GAMM Unreviewed; 335 AA.
AC A0A023Y9M0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=DX03_20425 {ECO:0000313|EMBL:AHY60999.1};
OS Stenotrophomonas rhizophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=216778 {ECO:0000313|EMBL:AHY60999.1, ECO:0000313|Proteomes:UP000025222};
RN [1] {ECO:0000313|EMBL:AHY60999.1, ECO:0000313|Proteomes:UP000025222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14405 {ECO:0000313|Proteomes:UP000025222};
RA Alavi P., Starcher M.R., Thallinger G., Zachow C., Mueller H., Berg G.;
RT "Is there a border between beneficial and pathogenic bacteria?";
RL Submitted (APR-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}.
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DR EMBL; CP007597; AHY60999.1; -; Genomic_DNA.
DR RefSeq; WP_038691577.1; NZ_QFBN01000013.1.
DR AlphaFoldDB; A0A023Y9M0; -.
DR STRING; 216778.DX03_20425; -.
DR GeneID; 61478268; -.
DR HOGENOM; CLU_026673_3_0_6; -.
DR OrthoDB; 9785812at2; -.
DR Proteomes; UP000025222; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 17..332
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 335 AA; 35907 MW; 2D31F532D2C5328A CRC64;
MKAVAYTEHG LPISDPRALQ DVTLPIPQPG PRDLRVAVRA ISVNPVDTKV RNGVAVTEPR
VLGWDAVGIV DAVGDEVTLF QPGDAVFYAG AIGRPGSNAE YQLVDERIVG HKPASLDDAA
AAALPLTAIT AWELLFDRLR IAEGGGEGQT LLVVGAAGGV GSILVQLARQ LTRLTVIGTA
SRPDTQDWVY GLGAHHVIDH SQPLTDGLQR LGIAEVSHVA SLTHTDQHYD QIVAALAPQG
QLALIDDPGQ LDVMALKRKS LSLHWESMFT RSSFNTPDLQ RQHDLLERVA ALVDAGVLRT
TLGEHYGRIN AANLRQAHAL IESHRARGKL VLEGF
//
