ID A0A2J7PU79_9NEOP Unreviewed; 515 AA.
AC A0A2J7PU79;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 03-MAY-2023, entry version 14.
DE RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN Name=ALDH7A1_3 {ECO:0000313|EMBL:PNF19876.1};
GN ORFNames=B7P43_G12529 {ECO:0000313|EMBL:PNF19876.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF19876.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF19876.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF19876.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:PNF19876.1}.
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DR EMBL; NEVH01021208; PNF19874.1; -; Genomic_DNA.
DR EMBL; NEVH01021208; PNF19876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7PU79; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR CDD; cd07130; ALDH_F7_AASADH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000235965}.
FT DOMAIN 38..498
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 515 AA; 55379 MW; C08E2941F69D8C83 CRC64;
MSISPLINDP KYSFLRNELD LKEENNGVFD GTWFGNGDVI TSVCPANGHE IAKVRAGNIS
DYNRCVEAAQ QAWCSWADLP APRRGEIVRQ IGDALRSKLE PLGKLVSLEM GKIQTEGVGE
VQEYVDVCDF ACGLSRTLKG QLLPSERPGH VLLENWNSLG VIGVISAFNF PIAVYGWNSA
IAMVCGNSVL WKGAPSTPLV SVATTKVVSG VLEANGIPGA VCCLCSGGSD IGETMARDTR
LPLLSFTGST QVGHQVGMLV QERFGRHLLE LGGNNALIVH HDADLDMMVR AAVFACVGTA
GQRCTTTRRL ILHTKVYNQV LTRLKAAYTQ VLLRVGDPLD KRTLIGPLHS AAAVRNYQDA
ISEAVEAGGT VEFGGKVIQR PGFFVEPTIV TGLPHNASVV HKETFAPIVY VLKAESLDQA
IMWNNEVHQG LSSSLFTASL DSIFKWIGPK GSDCGIVNVN IPTSGAEIGG AFGGEKHTGG
GRESGSDSWK QYMRRSTVTI NYSKELPLAQ GIRFE
//
