ID B5XXQ8_KLEP3 Unreviewed; 482 AA.
AC B5XXQ8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative succinate-semialdehyde dehydrogenase (NAD(P)(+)) {ECO:0000313|EMBL:ACI07579.1};
GN OrderedLocusNames=KPK_3548 {ECO:0000313|EMBL:ACI07579.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI07579.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI07579.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI07579.1,
RC ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000964; ACI07579.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XXQ8; -.
DR KEGG; kpe:KPK_3548; -.
DR HOGENOM; CLU_005391_5_1_6; -.
DR BioCyc; KPNE507522:GI0B-3531-MONOMER; -.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; 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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
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 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}.
FT DOMAIN 19..477
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 482 AA; 51481 MW; DDFF72D384B8C3EA CRC64;
MSVFHSDLFR QQALIAGSWR DAADGTTLAV SNPSTGTTLG QIPNMGRAEA QQAVDAAAVA
LPAWRALTAA QRATLLKNWH RLILENKTAL AQIMTAEQGK PLAEAEGEIA YAASFIEWFA
EQGKRTNGEI IPSPGADKRL MVIRQGVGVC AAITPWNFPA AMITRKAGPA LAAGCTMVIK
PANETPFTAL AMAELANQAG IPQGVINVVT GQSREIGAVF TGDERVRKLS FTGSTEVGRV
LMRQCAESIK KLSLELGGNA PFIVFDDADI DKAVEGALIA KFRNAGQTCV CVNRFYIHRA
VYDQFCDKFV ARVAALKVGD GSESDVQIGP LINADAGRKV QSLLDDALTR GATLLTGGKA
HPLGGNFFTP TVIGDVQPGS LLLQEEIFGP VAALVKFDDE QQVIEQANNT IYGLASYFYS
NDAARIWRVS EQLEYGMVGI NTGLISNEVA PFGGVKQSGL GREGSEHGIE DYLEMKYLCQ
GL
//
