ID H0PUS0_9RHOO Unreviewed; 339 AA.
AC H0PUS0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:BAL24271.1};
GN Name=adhA {ECO:0000313|EMBL:BAL24271.1};
GN ORFNames=AZKH_1958 {ECO:0000313|EMBL:BAL24271.1};
OS Azoarcus sp. KH32C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL24271.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL24271.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL24271.1,
RC ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AP012304; BAL24271.1; -; Genomic_DNA.
DR RefSeq; WP_015435576.1; NC_020516.1.
DR AlphaFoldDB; H0PUS0; -.
DR STRING; 748247.AZKH_1958; -.
DR KEGG; aza:AZKH_1958; -.
DR PATRIC; fig|748247.4.peg.1916; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_4; -.
DR OrthoDB; 5484143at2; -.
DR Proteomes; UP000007106; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007106};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..337
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 339 AA; 35360 MW; 6024006AE63B0B4F CRC64;
MKVVQFTDVG SPLKLADAPR PVAGPGELVF KVAACGVCAS DLHAAEVPGM LQVGNVLGHE
YSGVVAEVGP GVEGWLPGDR MIAIPVRPCG ACAACRSAQY MQCSDPMLQG FDPRLPGAYA
EYASCLAALA FKIPDGLGSV DAATVEPLAV GLGAWKTAQV PDGADVMIVG AGIIGLSIAK
WAKFFGAGCV GVSEMVPARM ERARQVGADV VIDAGACADP VAEYERQTGR KPSVIFECVG
RPMIARLIAM APIGTHLVLV GTGMENESFT VLSAAMKRLR MTFTLGYEPA DFGFVLQMLG
NGRITNAPMV TATIGLDELP ATFEVLRKPN DHCKVVVTP
//