ID   G0HS92_HALHT            Unreviewed;       481 AA.
AC   G0HS92;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AEM55918.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:AEM55918.1};
GN   Name=aldY3 {ECO:0000313|EMBL:AEM55918.1};
GN   OrderedLocusNames=HAH_0292 {ECO:0000313|EMBL:AEM55918.1};
OS   Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182
OS   / NCIMB 2187 / VKM B-1755).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=634497 {ECO:0000313|EMBL:AEM55918.1, ECO:0000313|Proteomes:UP000005629};
RN   [1] {ECO:0000313|EMBL:AEM55918.1, ECO:0000313|Proteomes:UP000005629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 /
RC   VKM B-1755 {ECO:0000313|Proteomes:UP000005629};
RX   PubMed=21994921; DOI=10.1128/JB.05953-11;
RA   Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., Wang S.,
RA   Xiang H.;
RT   "Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for
RT   studying genetics, metabolism, and virus-host interaction.";
RL   J. Bacteriol. 193:6086-6087(2011).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP002921; AEM55918.1; -; Genomic_DNA.
DR   RefSeq; WP_014039292.1; NC_015948.1.
DR   AlphaFoldDB; G0HS92; -.
DR   STRING; 634497.HAH_0292; -.
DR   GeneID; 25155970; -.
DR   KEGG; hhi:HAH_0292; -.
DR   eggNOG; arCOG01252; Archaea.
DR   HOGENOM; CLU_005391_1_0_2; -.
DR   OrthoDB; 6342at2157; -.
DR   Proteomes; UP000005629; Chromosome I.
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   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; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-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|RuleBase:RU003345,
KW   ECO:0000313|EMBL:AEM55918.1}.
FT   DOMAIN          16..477
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   481 AA;  50724 MW;  837DA8E6FC379C14 CRC64;
     MTQTYENYIG GEWTGSGETQ DVTNPADETD VVSTVPVASA ADADEAVAAA AEATDEWGGM
     SGPERGVLLR ETGEILKSRK DELAETLTRE EGKPLGEAEG EVQRAIDIFY YYAEKARDFG
     GTVKQPSGGR AGLQTKKEPM GVAALITPWN YPIAIPAWKI APALAVGNTV VIKPAMQAPT
     VGAMIVEALD EAGIPDGAIN LVCGPGSEVG ERLTTHEDVD VVSFTGSAAV GEHVYEQATS
     NGKRAQAEMG GKNPTVVMPS ADVDKAADIV GAGAFGGTGQ ACTATSRAIV HEDVYDEFLD
     AVVDYAESLE IGNGLDRAGM GPHVSEDELA GSLEYIDIAQ SEGATLETGG EELAGGEYDA
     GNFISPAVFS DVEPDMRIAQ EEVFGPVLAV IPVSDFDEGV EVANDIDYGL SASIVTDRIE
     EENEFIERSE SGVVKVNEKT TGLELHVPFG GLKRSSTNTY REQGDAGLEF FSYIKTVYRN
     S
//