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Database: UniProt
Entry: V6M546_9BACL
LinkDB: V6M546_9BACL
Original site: V6M546_9BACL 
ID   V6M546_9BACL            Unreviewed;       480 AA.
AC   V6M546;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   Name=gabD {ECO:0000313|EMBL:EST53689.1};
GN   ORFNames=T458_23275 {ECO:0000313|EMBL:EST53689.1};
OS   Brevibacillus panacihumi W25.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST53689.1, ECO:0000313|Proteomes:UP000017973};
RN   [1] {ECO:0000313|EMBL:EST53689.1, ECO:0000313|Proteomes:UP000017973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W25 {ECO:0000313|EMBL:EST53689.1,
RC   ECO:0000313|Proteomes:UP000017973};
RX   PubMed=24459276;
RA   Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT   "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT   Halotolerant Hydrocarbon-Degrading Bacterium.";
RL   Genome Announc. 2:e01215-13(2014).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EST53689.1}.
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DR   EMBL; AYJU01000017; EST53689.1; -; Genomic_DNA.
DR   RefSeq; WP_023558449.1; NZ_KI629785.1.
DR   AlphaFoldDB; V6M546; -.
DR   STRING; 1408254.T458_23275; -.
DR   PATRIC; fig|1408254.3.peg.4572; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_5_1_9; -.
DR   OrthoDB; 20170at2; -.
DR   Proteomes; UP000017973; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017973}.
FT   DOMAIN          13..476
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   480 AA;  52456 MW;  246EDD52A823118B CRC64;
     MGESKQMYIN GEWVSAESGE TLAVINPATC EQVGTVSFGD AREAKKAIDA AHEAFQSWSR
     LTARERSKYL STLAELVRKN RDELAGLISA EMGKPLGEAK GEVLGAADNF VWYSEEAKRV
     YGETIPSSVA NKRIMVLRQP VGVVGAITPW NFPINMVVRK IAPALAAGCT VVLKPAESTP
     LTAVRLFELI EQAGFPKGVV NLVVGNAESV GGEFLDNPKL SKIAFTGSTR VGKLLMEGAA
     KQVKRVSMEL GGHAPFIVFA DADLDAAVKG LFESKFRNSG QMCICTNRLY VHEEVADAFT
     EKLVERLKRA KVGDGREKET EIGPLVNERA LNKVLEHIED ARDKGAHVVF GGNRMTEGDY
     AKGFFCEPTV ISNVTTDMKI TYEETFGPVV PIVRFTDEAE VVRQANDTRY GLAAYVYTRD
     NQRCFRMAEE LEYGIVGIND GSPTQTQAPF GGFKESGIGR EGGRFGMDEY LETKFVSFGL
//
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