ID   A6VLA0_ACTSZ            Unreviewed;       339 AA.
AC   A6VLA0;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:ABR73747.1};
GN   OrderedLocusNames=Asuc_0369 {ECO:0000313|EMBL:ABR73747.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR73747.1, ECO:0000313|Proteomes:UP000001114};
RN   [1] {ECO:0000313|Proteomes:UP000001114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC   {ECO:0000313|Proteomes:UP000001114};
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR73747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VLA0; -.
DR   STRING; 339671.Asuc_0369; -.
DR   KEGG; asu:Asuc_0369; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_6; -.
DR   OrthoDB; 9773078at2; -.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd08261; Zn_ADH7; 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; 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:UP000001114};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          5..337
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   339 AA;  36525 MW;  DC252E2656B915B4 CRC64;
     MKAITVSQPF ELTVADVPAP TVTKDDDVII KVAFGGICGS DIGIYTGGNS LAKYPAIIGH
     EFVGTVVETG KAVTHVKVGD YVVSDIVNSC GHCYACRTGH HNVCKNLQVT GVHSQGGFAE
     YAKTRADNVY LVDTNKIPHK TACLIEPYAV GVEINTRASI AAGDKVVVFG SGPAGLAVMQ
     VARARGAEVL ITDIFEERLQ LAREMGATKA INVKDIDMRQ AVNEFTDDEG AHVVVDAVCS
     PQSILDALDI VAPSGRLVVL GTGAAPSEIP QVAFTKKGIN VFGTRLNNKR FPEVIRLFEE
     HKVTPEKMIT HTYKFEDIEK AFDVIKNEKN TVCKVLLEW
//