ID   Q2S1N2_SALRD            Unreviewed;       529 AA.
AC   Q2S1N2;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Aldehyde dehydrogenase (NAD) family protein {ECO:0000313|EMBL:ABC45185.1};
GN   OrderedLocusNames=SRU_1782 {ECO:0000313|EMBL:ABC45185.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC45185.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC45185.1, ECO:0000313|Proteomes:UP000008674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31
RC   {ECO:0000313|Proteomes:UP000008674};
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000159; ABC45185.1; -; Genomic_DNA.
DR   RefSeq; YP_445899.1; NC_007677.1.
DR   AlphaFoldDB; Q2S1N2; -.
DR   STRING; 309807.SRU_1782; -.
DR   EnsemblBacteria; ABC45185; ABC45185; SRU_1782.
DR   KEGG; sru:SRU_1782; -.
DR   PATRIC; fig|309807.25.peg.1850; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_10; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000008674; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07131; ALDH_AldH-CAJ73105; 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; 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; PS00070; ALDEHYDE_DEHYDR_CYS; 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:UP000008674}.
FT   DOMAIN          47..510
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   529 AA;  56671 MW;  EB48BEF6A78D849D CRC64;
     MPTGRRTTDC TLKFSAPRFG KALFPSKLSL FVSGMPDTFE NYIGGRWTGA ASQATFDNRN
     PADPDDHIGD FPDSAPADVD AAVQAAQDAF SDWGSTPAPD RGKILKASGD LLAERKDEIA
     RSMTREMGKP FFETKGDVQE AIDTAYYAAS ETRRLFGTTV PSELPDKMNM AIRRPLGVCG
     IITAWNFPVA VPSWKIFPAL AAGNTIVFKP SEDAPHSGLR FVQTLIDAGI PDGVINVVHG
     ADEAGQALVE HPEVDAIGFT GSYEVGTAIA ETCGRLNTPV SLEMGGKNPM IVMDDADLDL
     ALEGAIWGAY GTTGQRCTAT SRLICHESVH DELVAMIRDE AEALVLGDGN DADTDVGPLI
     NQAAAETVHR YVEIGQEEGA TLEMGGAPAS VDGLDGHFYE PTLFTDVTPD MTIAQEEIFG
     PVLATFEVGS YDEAVTVAND TQYGLSSSIY TQDVNKSFRA MRDLEAGITY VNGPTIGAEA
     HMPFGGVKDT GNGQRDGGYA AFEFWTEHKT LYVDYSGQLQ KAQMDSVED
//