ID   A7HXI3_PARL1            Unreviewed;       361 AA.
AC   A7HXI3;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Alcohol dehydrogenase zinc-binding domain protein {ECO:0000313|EMBL:ABS64616.1};
GN   OrderedLocusNames=Plav_3009 {ECO:0000313|EMBL:ABS64616.1};
OS   Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Parvibaculaceae; Parvibaculum.
OX   NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS64616.1, ECO:0000313|Proteomes:UP000006377};
RN   [1] {ECO:0000313|EMBL:ABS64616.1, ECO:0000313|Proteomes:UP000006377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC   {ECO:0000313|Proteomes:UP000006377};
RX   PubMed=22675581; DOI=10.4056/sigs.2215005;
RA   Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA   Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA   Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT   "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT   1(T)).";
RL   Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS64616.1; -; Genomic_DNA.
DR   RefSeq; WP_012111937.1; NC_009719.1.
DR   AlphaFoldDB; A7HXI3; -.
DR   STRING; 402881.Plav_3009; -.
DR   KEGG; pla:Plav_3009; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_5; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000006377; 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:UP000006377};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..357
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  38499 MW;  DE6E4D2AF6278BBA CRC64;
     MKAAVLRQVG QPLAIEDVKI NKPGPHEVLI RTVAAGVCHS DLHFVEGSYP YPLPAVLGHE
     SAGVVEQVGS EVRTVKPGDH VITCLSAFCG HCEHCLTGHL SRCVSPETKR QAEEEPRLGA
     VPGAMNQFLN LSSFAEQMLI HEHACVAIRK DMPLDRAALI GCSVTTGVGA VIHTSNVRPG
     ETVAVLGCGG VGLACINGAA IAGAGRIIAI DTQGSKLNLA KEFGATDVVN AKDGDPVKQV
     MDLTNGGVHH SFEAIGLKAT TEQAFRMLAR GGTANVIGMI PVGVHIELHG ADFLGEKRIQ
     GSTMGSNRFP VDMPRFVDFY MSDKLKLDQM ISRRIKLDQV NEAFDELKRG ELARSVIMFD
     A
//