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Database: UniProt
Entry: M1XNS2_NATM8
LinkDB: M1XNS2_NATM8
Original site: M1XNS2_NATM8 
ID   M1XNS2_NATM8            Unreviewed;       478 AA.
AC   M1XNS2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:CCQ35601.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:CCQ35601.1};
GN   Name=aldH2 {ECO:0000313|EMBL:CCQ35601.1};
GN   OrderedLocusNames=Nmlp_1397 {ECO:0000313|EMBL:CCQ35601.1};
OS   Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS   8.8.11).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ35601.1, ECO:0000313|Proteomes:UP000011867};
RN   [1] {ECO:0000313|EMBL:CCQ35601.1, ECO:0000313|Proteomes:UP000011867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC   {ECO:0000313|Proteomes:UP000011867};
RX   PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA   Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA   Gross K., Schuster S.C., Oesterhelt D.;
RT   "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT   of a previously haloalkaliphilic genus.";
RL   Genome Announc. 1:e0009513-e0009513(2013).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; HF582854; CCQ35601.1; -; Genomic_DNA.
DR   RefSeq; WP_015408447.1; NC_020388.1.
DR   AlphaFoldDB; M1XNS2; -.
DR   STRING; 268739.Nmlp_1397; -.
DR   GeneID; 14650684; -.
DR   KEGG; nmo:Nmlp_1397; -.
DR   eggNOG; arCOG01252; Archaea.
DR   HOGENOM; CLU_005391_1_0_2; -.
DR   OrthoDB; 6342at2157; -.
DR   Proteomes; UP000011867; 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; cd07078; ALDH; 1.
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; PTHR42991; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42991:SF1; 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   ECO:0000313|EMBL:CCQ35601.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011867}.
FT   DOMAIN          18..476
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   478 AA;  50129 MW;  F80603843BF05DA6 CRC64;
     MATDSTLNHD ELYIEGRWTP TADRIDVTDL TDDTTFASVS AATPADAEDA LAAAQAAEVE
     MRETTVVQRA EWVTAIADGI EARKAELADV IVREAGKPIS SARGEVDAAA ERFRRAAEEA
     RSLKGEYIEG TTEGHEGWRA IVRHEPVGTA LCITPYNYPL STTALQVAPA LAAGNAVILK
     PASKTPISAA ILAEIIVDAA DDLPEGAFGF VPGRASEIGD VLAGDDRIDA IAMTGSSGAG
     KHVAGVSGMV ELHMELGGNA PAIVFPDADL EAASSAAASG SLKYAGQRCS AVSRVLVHED
     AHDELVDRID AEMDGFEPGD LFDEETSLGP LISHEQAEWV EELVEDALDR GATLVRGGAR
     SGRFFEPTLL ADVPQDARIV HEEQFGPVVA VTTFDDEAGA LEVANGGSLG LDAAVFTADY
     DRAMRVADRL EVGGVRINGA PSHGLGDIPF GGTKDSGIGR EGIGYTIEAF LERKSIIL
//
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