ID A0A024P5M5_9BACI Unreviewed; 506 AA.
AC A0A024P5M5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Putative aldehyde dehydrogenase AldA {ECO:0000256|ARBA:ARBA00039869};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN Name=thcA {ECO:0000313|EMBL:CDQ23267.1};
GN ORFNames=BN983_01490 {ECO:0000313|EMBL:CDQ23267.1};
OS Halobacillus karajensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=195088 {ECO:0000313|EMBL:CDQ23267.1, ECO:0000313|Proteomes:UP000028868};
RN [1] {ECO:0000313|EMBL:CDQ23267.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ23267.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ23267.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ23267.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Halobacillus karajensis HK-03.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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:CDQ23267.1}.
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DR EMBL; CCDI010000001; CDQ23267.1; -; Genomic_DNA.
DR RefSeq; WP_035506937.1; NZ_FNWW01000001.1.
DR AlphaFoldDB; A0A024P5M5; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000028868; 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 CDD; cd07116; ALDH_ACDHII-AcoD; 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; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-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:UP000028868}.
FT DOMAIN 27..493
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 506 AA; 56315 MW; 15D696720BFFF704 CRC64;
MVYAFPNTEG SKVQFKERYD NFIGGEWTAP VKGQYFDNVT PVTGKNFCQV ARSTEEDVEL
ALDAAHKAKD VWGKTSVTER SLILNRIADR MEENLEKLAI AETWENGKAV RETLNADLPL
AIDHFRYFAS VIRSQEGSIG EIDNDTVAYH FHEPLGVVGQ IIPWNFPLLM ATWKIAPALA
AGNAIVLKPA EQTPASILYL LEMIEDLLPA GVLNVINGFG LEAGKPLAQS PRINKVAFTG
ETTTGRMIMQ YASQNIIPVT LELGGKSPNI IFEDVMREDD DFLDKTIEGM VMFALNQGEV
CTCPSRALIQ ESIYDEFIER AIKRVKEIKV GNPLDPEVMM GAQASSEQLE KILSYLDIGK
DEGAECLAGG ARNQMEGDLK EGYYVQPTVF KGNNSMRIFQ EEIFGPVLSV TTFKDKEEAM
EIANDTLYGL GAGVWTRDMN TAYRFGRGIE AGRVWTNCYH AYPAHAAFGG YKMSGVGREN
HKMMLSHYQQ TKNMLVSYSP QKLGFF
//
