ID   D5BDR7_ZUNPS            Unreviewed;       517 AA.
AC   D5BDR7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   OrderedLocusNames=ZPR_0298 {ECO:0000313|EMBL:ADF50658.1};
OS   Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS   profunda).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zunongwangia.
OX   NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF50658.1, ECO:0000313|Proteomes:UP000001654};
RN   [1] {ECO:0000313|EMBL:ADF50658.1, ECO:0000313|Proteomes:UP000001654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC   {ECO:0000313|Proteomes:UP000001654};
RX   PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA   Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA   Zhou B.C., Yu J., Zhang Y.Z.;
RT   "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT   to the deep-sea environment and ecological role in sedimentary organic
RT   nitrogen degradation.";
RL   BMC Genomics 11:247-247(2010).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP001650; ADF50658.1; -; Genomic_DNA.
DR   RefSeq; WP_013069811.1; NC_014041.1.
DR   AlphaFoldDB; D5BDR7; -.
DR   STRING; 655815.ZPR_0298; -.
DR   KEGG; zpr:ZPR_0298; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_2_10; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000001654; Chromosome.
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}.
FT   DOMAIN          37..498
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   517 AA;  56091 MW;  BC05870950A88F18 CRC64;
     MSQIAKDFGI DKALEELGLQ DINNGTSTGK DFFSGGEIIE SYSPVDGALI GKVKATTPED
     YEKVITTAEK AFKEWRTMPA PQRGEIVRKF NDELRRLKEP LGKLVSYEMG KSYQEGLGEV
     QEMIDICDFA VGLSRQLHGL TMHSERPGHR MYEQYHPLGV VGIISAFNFP VAVWSWNTAL
     AWVCGDACIW KGSEKTPLTS VACQNIAARV FSENGVPEGI SCLITGDYKV GELMTKDERI
     PLISATGSTR MGKTVAKEVA GRLGKSLLEL GGNNAIIVTP DANIKNTVIG AVFGAVGTCG
     QRCTSTRRLV VHEDVYDKVK NAIVDAYQQI KIGNPLDENN HVGPLIDKDA VKNYQAALEK
     VVEEGGKVLV EGGVLEGEGY ESGCYVKPAI AEAENHFEIV QHETFAPVLY IMKYKGDVSN
     ALELQNGVRQ GLSSAIMTNN LREAERFLSV EGSDCGIANV NIGTSGAEIG GAFGGEKETG
     GGRESGSDAW KVYMRRQTNT INYTTELPLA QGIKFDL
//