ID A0A0L0H4D6_9ENTR Unreviewed; 499 AA.
AC A0A0L0H4D6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:KNC95568.1};
GN ORFNames=GM31_00460 {ECO:0000313|EMBL:KNC95568.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC95568.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC95568.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC95568.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(2015).
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:KNC95568.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNGI01000011; KNC95568.1; -; Genomic_DNA.
DR RefSeq; WP_049855709.1; NZ_JNGI01000011.1.
DR AlphaFoldDB; A0A0L0H4D6; -.
DR STRING; 379893.GCA_001297775_04146; -.
DR PATRIC; fig|379893.4.peg.95; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000037393; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000037393}.
FT DOMAIN 32..495
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 499 AA; 53408 MW; F6AE4ACAB2017D70 CRC64;
MSGSQVATLA SVQMFLDRQH GLYIDGGQQA AQSEKRLTIY NPATGEPIAT TADASAADVD
KAVMSAWKAF VARTWAGRLP AERERILLRF ADLVEQHTEE LAQLETLEQG KSIHIARAFE
VGCTLNWMRY TAGLTTKITG STLDVSIPMP AGARYQAWTK KEPVGVVAGI VPWNFPLMIG
MWKVMPALAA GCSIVIKPSE TTPLTLLRVA ELATEAGIPD GVFNVVTGSG SECGAALTSH
PQVAKVSFTG STATGKQIAR SAADRLTRVT LELGGKNPAI VLKDADPQWV IEGLMTGSFL
NQGQVCAASS RIYIEAPLFD NLVSGFEQAV KSLNVGPGMS ETAHINPLVS RAHCDKVQAF
LQEAQQNNAE LLSGNAGPGG NGYYVAPTLV VNPDASLRLT REEVFGPVVN LVRVADGKEA
LRLANDTEYG LTASVWTRDL SQALSFSDRL QAGTVWINSH TLIDANLPFG GMKQSGTGRD
FGPDWLDGWC ETKSVCVRY
//