ID G4F161_9GAMM Unreviewed; 336 AA.
AC G4F161;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=HAL1_00485 {ECO:0000313|EMBL:EHA17661.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA17661.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA17661.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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:EHA17661.1}.
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DR EMBL; AGIB01000001; EHA17661.1; -; Genomic_DNA.
DR RefSeq; WP_008956040.1; NZ_CP130610.1.
DR AlphaFoldDB; G4F161; -.
DR PATRIC; fig|550984.5.peg.97; -.
DR Proteomes; UP000005692; 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 13..333
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 336 AA; 36250 MW; A94201B35F8B2ECE CRC64;
MKAIAFTQSL PIDHPDALQE IELPIPTPEA HDIRVAVSAV SVNPVDAKVR NSALPQTGEP
RVLGYDAVGI VDAVGSAVTR FQPGDRVWYA GNIARQGSNA EFQLVDERIA SLAPKSLSDT
EAAALPLTAI TAWELLFDRL ELGMRDTQGK SLLVIGAAGG VGSILVQLAK QLTDITVIGT
ASRPESQAWV KSLGADAVIN HHQPLDQELK AAGFDGVDMV ISLNQTDHHF EAIIEALKPQ
GKLALIDDPE LIDVRKLKMK SLSLHWELMF TRPLFATDDL AKQHDLLTKV AAMVDDGRLK
TTLGEVLGPI NAENLKRAHA LIESNRTIGK LVLEGF
//
