ID A0A0Q5TPD6_9SPHI Unreviewed; 336 AA.
AC A0A0Q5TPD6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=ASG14_12555 {ECO:0000313|EMBL:KQS36248.1};
OS Pedobacter sp. Leaf194.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS36248.1, ECO:0000313|Proteomes:UP000051708};
RN [1] {ECO:0000313|EMBL:KQS36248.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS36248.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS36248.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS36248.1,
RC ECO:0000313|Proteomes:UP000051708};
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:KQS36248.1}.
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DR EMBL; LMPU01000009; KQS36248.1; -; Genomic_DNA.
DR RefSeq; WP_056871603.1; NZ_LMPU01000009.1.
DR AlphaFoldDB; A0A0Q5TPD6; -.
DR STRING; 1736297.ASG14_12555; -.
DR OrthoDB; 648910at2; -.
DR Proteomes; UP000051708; 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; 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 11..334
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 336 AA; 37302 MW; F55F17AEE17438DB CRC64;
MKAIGFKKSL PVIEEESFIT FQTEKPTAKG RDLLVRITAI SVNPVDYKVR QNSAKDKVLE
QPKVIGWDAV GEVEETGPEV SLFQKGDVVY YAGDLNRSGS NAEYQLVDER IVGRKPENLT
PAQAAAMPLT LLTAWEILFD RIRINERDKG KSLLIIGGAG GVGSIAIQIA KKVAGLTVLA
TASRPESVEW CRRQGADFVV NHQNLVQEVQ QAGFNQVDFI VDFVDVNQYW DAMVTLIKPQ
GHIGSISDPV ENVNLRQLKG KSVSFHWELM FTRSMFQTQD IIRQHHILTE AAALFENGTI
NSTINEHLTG FSTENLKQAH ALLESGKTIG KIVIEY
//
