ID A0A2T1LT51_9CHRO Unreviewed; 334 AA.
AC A0A2T1LT51;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:PSF33617.1};
GN ORFNames=C7H19_19720 {ECO:0000313|EMBL:PSF33617.1};
OS Aphanothece hegewaldii CCALA 016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=2107694 {ECO:0000313|EMBL:PSF33617.1, ECO:0000313|Proteomes:UP000239001};
RN [1] {ECO:0000313|EMBL:PSF33617.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF33617.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSF33617.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF33617.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Keele B.F.;
RL Submitted (MAR-2018) 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}.
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:PSF33617.1}.
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DR EMBL; PXOH01000029; PSF33617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1LT51; -.
DR OrthoDB; 9770526at2; -.
DR Proteomes; UP000239001; 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:UP000239001};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 36071 MW; 5B50E27A16B4C965 CRC64;
MIRAYAASEP GGELTPYEYD PGQLGDEDVE IQVEYCGICH SDLSMLDNEW GMTQYPFIPG
HEVVGTIAAI GDHVKDRQIG QRVGLGWYSR SCMGCEWCMS GDHNLCLTAE GTIVGRHGGF
ADRVRAHHSW TTPLNDGVDP AKAGPLFCGG ITVFNPIVQF NIKPTDHVGV IGIGGLGHMA
LRFLKAWGCE VTAFSGSPDK EAEAKELGAT HFVNSRDPEA LKAIANSLDM ILSTVSADLP
WADYLATLRP KGRLHIVGVA PNPLSFHVFP MIAGQKSISG SPLGSPATVS KMLEFAARHG
VEPITELFPI SQVNEAIDKL RHGSPRYRLV LKVS
//