ID E5WP54_9BACI Unreviewed; 498 AA.
AC E5WP54;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:EFV75463.1};
GN ORFNames=HMPREF1013_04241 {ECO:0000313|EMBL:EFV75463.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV75463.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV75463.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV75463.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:EFV75463.1}.
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DR EMBL; ACWD01000061; EFV75463.1; -; Genomic_DNA.
DR RefSeq; WP_009335083.1; NZ_GL635755.1.
DR AlphaFoldDB; E5WP54; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_9; -.
DR Proteomes; UP000003283; 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 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:UP000003283}.
FT DOMAIN 28..494
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 498 AA; 53590 MW; 0F4C9CE93A389ED2 CRC64;
MSTEVNSQKT VAVNAGAETF YNYIGGEWVP SVTGETYPSV NPANTDEVLG YFQKSNEIDV
QKAIESAKRA FPEWKNTSPI SRGDILFKLI FLIQQEKEEL AEIITKEVGK TIGAARKEVD
ATVQALKHFS GEANRISGET VPAIDPKTFA CTIQEPLGVV AVVTPFNFPL GIAIYKIAPS
MLAGNTIIYK AASDTSLIAV KVVELFEKAG MPAGVLNMIT GPGSVVGEEL GTNPEIKAVS
FTGSSDVGIH LGKLVTAHGG KMQAEMGGKN ATIILEDANL EEAVQSVVIS GFYNNGQSCT
GTSRVIVPRS ISRKVIELLV EKAKQVKVGD GVREGNDNGA VANKHQLNTY LHYVNSAIEE
GAVLEYGGKQ LTDGDMANGY FVAPTVFSKV TKDFTIAQEE IFGPVVAVME VDSYEEAIEL
ANDTEFGLSS AIFTNDLQKA FDFVRKIETG VTHVNIPSNH YENQLPFGGK KTSSIGPREQ
GSTALDFWLD TKTVYIKP
//
