ID B4VJU2_9CYAN Unreviewed; 334 AA.
AC B4VJU2;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Alcohol dehydrogenase GroES-like domain family {ECO:0000313|EMBL:EDX77810.1};
GN ORFNames=MC7420_3134 {ECO:0000313|EMBL:EDX77810.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX77810.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX77810.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX77810.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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; DS989843; EDX77810.1; -; Genomic_DNA.
DR RefSeq; WP_006099071.1; NZ_DS989843.1.
DR AlphaFoldDB; B4VJU2; -.
DR STRING; 118168.MC7420_3134; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_3; -.
DR OrthoDB; 9770526at2; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF38; ALDEHYDE REDUCTASE AHR; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000003835};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 35968 MW; 6B8ED4C836B61254 CRC64;
MIKAYAAHEP GGQLQPFEYD PGTLGDEEVE IKVEYCGICH SDLSMLDNEW GMTDYPFVPG
HEVVGTIAAL GDKVTTLNLG QRVGLGWFSG SCMTCEWCMS GNHNLCSNAE GTIVSRHGGF
ADKVRADYSW VVPLPDGINP ATAGPLFCGG ITVFNPIVQF DIKPSDRVGV IGIGGLGHIA
LGFLQAWGCE ITAFSSSPDK EAEARELGAT HFINSGDVNA LESVQNSFDF ILATANADLD
WNAYIAALRP KGRLHFVGVI PNPLSTPIFP LILGQKSISA SPVGSPATIS QMINFAARQG
VEPITETFSF EQVNEAMEKL RHGKPRYRLV LKHS
//