ID A0A0K9NUT6_ZOSMR Unreviewed; 495 AA.
AC A0A0K9NUT6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydroxycinnamaldehyde dehydrogenase {ECO:0000313|EMBL:KMZ59710.1};
GN ORFNames=ZOSMA_65G00420 {ECO:0000313|EMBL:KMZ59710.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ59710.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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:KMZ59710.1}.
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DR EMBL; LFYR01001739; KMZ59710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NUT6; -.
DR STRING; 29655.A0A0K9NUT6; -.
DR OMA; KCAKAMR; -.
DR OrthoDB; 3078548at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF304; CYTOSOLIC ALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT DOMAIN 24..485
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 495 AA; 53424 MW; 7D6F619FD4B1FF58 CRC64;
MSTEGKMKMP DIKFTKLFID GEFVDAISGK TFETIDPRSG EVIARVAEGD MADINLAVKS
AREAFDHGEW PRMSGAQRGR IMMRFADLID EHTDELAALD AIDAGKLLSM CKIADVPGSA
GNLRYYAGAA DKIHGETLKM TMNYQGYTLK EPIGVVGGII PWNFPIFMFS MKVSPALAVG
CTIVLKPAEQ TPLSALYCAH LAKEAGIPDG VLNVVPGFGS TAGSALASHM DVDKILFTGS
TEVGRKIMEA SARSNLKPLS LELGGKSPLV IFDDADVDMA TNLAQIASFT NKGEICIAGS
RVFVQEGIYD EFLKKAVEKA ESLKVGDPFH VDTNQGPQVD KIQFQKVLSY IESGRTDGAT
LATGGSRCGD KGYYIQPTIF TDVKDDMMIA KDEIFGPVMS LMKFKTTEEA IERANDTKYG
LAAGVVTNDI NIMNQVSRSI RAGVIWVNCY LASGPDCPFG GYKMSGFGSD QGMDALDGVL
KKKSIVTPIY KTPWL
//
