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Database: UniProt
Entry: B8J2V8_DESDA
LinkDB: B8J2V8_DESDA
Original site: B8J2V8_DESDA 
ID   B8J2V8_DESDA            Unreviewed;       502 AA.
AC   B8J2V8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:ACL49877.1};
GN   OrderedLocusNames=Ddes_1981 {ECO:0000313|EMBL:ACL49877.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49877.1};
RN   [1] {ECO:0000313|EMBL:ACL49877.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL49877.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) 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; CP001358; ACL49877.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8J2V8; -.
DR   STRING; 525146.Ddes_1981; -.
DR   KEGG; dds:Ddes_1981; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_1_7; -.
DR   OMA; VWTRDAH; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
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}.
FT   DOMAIN          27..489
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   502 AA;  55222 MW;  9C52B8AF36FCD06F CRC64;
     MQTFNQRKRH EKTDLQDRYS LFIDGEWKEA SDGGTFESLC PANGERLATC AEATREDVDA
     AVKAATTAWA SWKNTDAAER ADLLMKIADI IDANKEHLAL VETLDNGKPI RETANVDIPF
     AADHFRYFAG VLRSEEGSAT MLDKNTLSLV LREPIGVVGQ IVPWNFPFLM AAWKLAPVLA
     AGCCTVFKPS NHTSLSVLEL ARLINGVLPK GVFNVITGRG SRSGQYILEH PGFNKLAFTG
     STDVGRSVGM AAAKRLIPST LELGGKSANI FFPDCQWDLA MDGLQMGILF NQGQVCCAGS
     RVFVHEDIYD RFVAEAVERF NRVKVGLPWE ADTQMGSQIY ESHLKAILLC IEQAKGEGAT
     VLCGGERVTS GDLDRGCFMR PTLLGNVTND MRVARDEIFG PVAVIIKFKT EEEVVRMAND
     SVYGLGGGVW TRDINRAIRV SRAIETGRMW VNTYNSIPAG APFGGYKESG IGRETHKTIL
     EHYTQQKNII INLSEAPTRF YP
//
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