ID A0A087N2C3_9BACI Unreviewed; 474 AA.
AC A0A087N2C3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN Name=gabD {ECO:0000313|EMBL:KFL43276.1};
GN ORFNames=CH76_07770 {ECO:0000313|EMBL:KFL43276.1};
OS Lysinibacillus sp. BF-4.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL43276.1, ECO:0000313|Proteomes:UP000029097};
RN [1] {ECO:0000313|EMBL:KFL43276.1, ECO:0000313|Proteomes:UP000029097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL43276.1,
RC ECO:0000313|Proteomes:UP000029097};
RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H.,
RA Grass G.;
RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus isolated
RT during an anthrax outbreak in Bavaria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFL43276.1}.
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DR EMBL; JPUW01000018; KFL43276.1; -; Genomic_DNA.
DR RefSeq; WP_036144883.1; NZ_JPUW01000018.1.
DR AlphaFoldDB; A0A087N2C3; -.
DR eggNOG; COG1012; Bacteria.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000029097; Unassembled WGS sequence.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic 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 InterPro; IPR010102; Succ_semiAld_DH.
DR NCBIfam; TIGR01780; SSADH; 1.
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:UP000029097}.
FT DOMAIN 12..470
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 474 AA; 51372 MW; A6097601FA17FBD7 CRC64;
MKNYELLING EWVGKDWKQY EVINPATKQP MASVPYGGEA EAKAAVDAAA EAFTTWKKKT
AQERCDILYR WYELVKENEQ EIAALMTEEQ GKPLAEALGE VRYANAYIQW YAEEGKRVYG
ETIPASAPDK RMLVLRQPIG VVAAITPWNF PAAMITRKIA PALAVGCTAV LKPASQTPLT
AIKLVEYAEQ AGVPKGVINI VTGSAREIGG AWTSDSRVRK LTFTGSTEVG KQLMKDSADT
MKKVSLELGG HAPFIVLKDA DLEVAVAGVL ASKFRNAGQT CICTNRVYVH KDIEEKFVAL
VAEKVKAMKV GNGLDKTTDI GPMIDENAVD KVNEHVEDAR AKGAVVETGG KRATGDGYYY
EPTVMSGVTD DMQCMSEETF GPLLPIATFT DVDDAIARAN NTPFGLAAYV FTTNLSEAFY
VSEALEYGII GLNDGGPSAA QAPFGGWKES GTGREGGRQG MEDYLETKYI SIKL
//
