ID A0A1Q9D2X3_SYMMI Unreviewed; 407 AA.
AC A0A1Q9D2X3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Mannitol dehydrogenase {ECO:0000313|EMBL:OLP89529.1};
GN Name=MTD {ECO:0000313|EMBL:OLP89529.1};
GN ORFNames=AK812_SmicGene28985 {ECO:0000313|EMBL:OLP89529.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP89529.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP89529.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP89529.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC 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:OLP89529.1}.
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DR EMBL; LSRX01000754; OLP89529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9D2X3; -.
DR OMA; GTYNGPT; -.
DR OrthoDB; 1550at2759; -.
DR Proteomes; UP000186817; 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; 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:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..363
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 407 AA; 43580 MW; F4614FAB01E1730C CRC64;
MAEPVDMMVM ACKDPSCDFK PMKMKRRPLG DEDVLIDMVY CGVCHTDLHI AANHVGGLQA
TVYPCVPGHE LVGVCTRVGS KVTKVKVGDH VGVGCMVDSC MKCTGCKKGN ENLCRKQNTA
TYQGKDLHGR AATYPTGGVT MGGYCTKMVV HEHFAILIPK NYPLASAGPV MCAGVTMYEP
LRYWKAGPSS KVAVVGLGGL GMTGIKVAKA MGCQVTAISR GEKKKALAEK SGADGFISST
SPEQMQAACQ SFDLVLDTIP TEHDYTQYQK LAAVDGKCVL IGISNAFGGA IIVDAITGGR
STMSASMIGG VQSTQEIIDL CAKHNIVLDH KICPVWELGK IYEELDSSND QGLRYVLDLK
NTLNEDAEAK CTAPPPKLST PETAPSLRGI FGECFSMLFV HWNLKKI
//
