ID G1VPL2_9FIRM Unreviewed; 340 AA.
AC G1VPL2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=HMPREF9022_01943 {ECO:0000313|EMBL:EGX75444.1};
OS Erysipelotrichaceae bacterium 2_2_44A.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=457422 {ECO:0000313|EMBL:EGX75444.1, ECO:0000313|Proteomes:UP000003043};
RN [1] {ECO:0000313|EMBL:EGX75444.1, ECO:0000313|Proteomes:UP000003043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_2_44A {ECO:0000313|EMBL:EGX75444.1,
RC ECO:0000313|Proteomes:UP000003043};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium 2_2_44A.";
RL Submitted (JUN-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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:EGX75444.1}.
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DR EMBL; ADCZ01000020; EGX75444.1; -; Genomic_DNA.
DR RefSeq; WP_008727876.1; NZ_CP048838.1.
DR AlphaFoldDB; G1VPL2; -.
DR GeneID; 61928430; -.
DR PATRIC; fig|457422.3.peg.2043; -.
DR HOGENOM; CLU_026673_11_0_9; -.
DR OrthoDB; 9787435at2; -.
DR BioCyc; EBAC457422-HMP:GMFD-1965-MONOMER; -.
DR Proteomes; UP000003043; Unassembled WGS sequence.
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 CDD; cd08234; threonine_DH_like; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 340 AA; 37132 MW; C042A44DC7EF7BD2 CRC64;
MKAAVYFGRH DVRITDFKEP PLTDTGVKIA VSYCGLCGTD LHKYDGKGGS RPVIPPVVLG
HEASGVIVET GKSVSKFQVG ERVCVDPNWS CGHCACCQEG MTHMCENSRG VVKGFAQYIC
PPQENVYPIP DSLSLKHAAL AEPLSCCLHG MDLLDVHLGD HVLIVGMGAI GSMMVQLCRL
AGAAHIVVVE PQREKKELAV KLGATMFLSP DDDVIGILQQ EQLHISRVME CVGLKATIED
AFRYAGKCAT VVLFGLGDPQ HPAVFDQYSA FQKELTIKTS FVNPHTTQRA INLLSTKAID
CDAIISRIMP LEDVVEELRT QEWFRKGKVI VKIGGDMEER
//
