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Database: UniProt
Entry: Q0A521_ALKEH
LinkDB: Q0A521_ALKEH
Original site: Q0A521_ALKEH 
ID   Q0A521_ALKEH            Unreviewed;       506 AA.
AC   Q0A521;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Aldehyde dehydrogenase (NAD(+)) {ECO:0000313|EMBL:ABI58066.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:ABI58066.1};
GN   OrderedLocusNames=Mlg_2726 {ECO:0000313|EMBL:ABI58066.1};
OS   Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI58066.1, ECO:0000313|Proteomes:UP000001962};
RN   [1] {ECO:0000313|Proteomes:UP000001962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC   {ECO:0000313|Proteomes:UP000001962};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA   Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA   Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000453; ABI58066.1; -; Genomic_DNA.
DR   RefSeq; WP_011630459.1; NC_008340.1.
DR   AlphaFoldDB; Q0A521; -.
DR   KEGG; aeh:Mlg_2726; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_6; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000001962; 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; cd07116; ALDH_ACDHII-AcoD; 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   PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 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:UP000001962}.
FT   DOMAIN          27..493
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   506 AA;  55783 MW;  CFC0CFD324579E6B CRC64;
     MIYANPGERD AKVQFKPRYG NFINGEWVEP ASGQYFENIT PVTGEVFCEV ARSNADDVER
     ALDAAHAAKD AWGKASVTER ANVLLKIADR MEANLERLAV AETWDNGKPV RETLNADLPL
     AIDHFRYFAG AIRAQEGGIS EIDHDTIAYH FHEPLGVVGQ IIPWNFPLLM ATWKIAPALA
     CGNCIVLKPA EQTPASILVL MECIQDVLPP GVLNVVNGFG VEAGKPLATS NRIAKVAFTG
     ETTTGRLIMQ YAAENIIPVT LELGGKSPNI FMADVMDQDD DFLDKAIEGM TLACLNQGEV
     CTCPSRALIQ EDIYDDFIAK VIDRFSMVKQ GNPLDTETMI GAQASSEQME KILSYMDIGR
     QEGAECLIGG DRAEIGGDFQ NGYYVQPTLF RGHNKMRIFQ EEIFGPVVSV TTFKDEAEAL
     ELANDTLYGL GAGLWSRSAH TTYRMGRAIQ AGRVWTNCYH LYPAHAAFGG YKQSGIGREN
     HQMMLEHYQQ TKNLLVSYSP KAMGFF
//
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