ID   B4RGP3_PHEZH            Unreviewed;       361 AA.
AC   B4RGP3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Alcohol dehydrogenase class III {ECO:0000313|EMBL:ACG77259.1};
GN   Name=adhI {ECO:0000313|EMBL:ACG77259.1};
GN   OrderedLocusNames=PHZ_c0845 {ECO:0000313|EMBL:ACG77259.1};
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77259.1, ECO:0000313|Proteomes:UP000001868};
RN   [1] {ECO:0000313|EMBL:ACG77259.1, ECO:0000313|Proteomes:UP000001868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1 {ECO:0000313|EMBL:ACG77259.1,
RC   ECO:0000313|Proteomes:UP000001868};
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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; CP000747; ACG77259.1; -; Genomic_DNA.
DR   RefSeq; WP_012521407.1; NC_011144.1.
DR   AlphaFoldDB; B4RGP3; -.
DR   STRING; 450851.PHZ_c0845; -.
DR   KEGG; pzu:PHZ_c0845; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_5; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000001868; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08279; Zn_ADH_class_III; 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; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001868};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..357
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  38210 MW;  8377C2F24A892658 CRC64;
     MKAAVLREVR KPLQIEDVQI SKPGPHEVLI RTAAAGVCHS DLHFVEGSYP HPLPAVLGHE
     SAGVVEAVGS EVRTVKPGDH VITCLSAFCG HCEHCLTGHM SLCVSPDTKR GDEDEPRLTS
     PKGPMMQYLN LSSFAEQMLV HEHACVAIRK DMPLDRAALI GCSVMTGVGA VMHTSNVRPG
     DTVAVIGCGG VGLSAINGAA IAGAGRIIAI DVVPGKENFA RAFGATDFVN AAETDPVKAV
     IELTKGGVQH SFEALGMTKT AEQAFNMLRR GGTANIIGMI PVGQSISLMG AAFLGEKRIQ
     GSMMGSNRFP VDMPRLVDMY MAGKLKLDGM ISQRLKLEQV NEAFAEMKTG SIARSVIVFD
     A
//