ID Q8P5U1_XANCP Unreviewed; 526 AA.
AC Q8P5U1;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Ketoglutarate semialdehyde dehydrogenase {ECO:0000313|EMBL:AAM42514.1};
GN OrderedLocusNames=XCC3244 {ECO:0000313|EMBL:AAM42514.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM42514.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM42514.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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DR EMBL; AE008922; AAM42514.1; -; Genomic_DNA.
DR RefSeq; NP_638590.1; NC_003902.1.
DR RefSeq; WP_011038347.1; NC_003902.1.
DR AlphaFoldDB; Q8P5U1; -.
DR STRING; 190485.XCC3244; -.
DR EnsemblBacteria; AAM42514; AAM42514; XCC3244.
DR KEGG; xcc:XCC3244; -.
DR PATRIC; fig|190485.4.peg.3466; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_027555_0_0_6; -.
DR OrthoDB; 9770537at2; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR CDD; cd07129; ALDH_KGSADH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044151; ALDH_KGSADH.
DR PANTHER; PTHR43353:SF3; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT DOMAIN 38..460
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 526 AA; 54511 MW; DD357CCFBF9EB152 CRC64;
MHTILGESLI GQRSVQGAGV ALQGVDATTG EALQPVFGSA TAPDVEQACA LAQAAFDPYR
ETTLEARAQF LETIAEQILA LGDGLIERAM RESGLPRARL EGERGRTVGQ LRLFASVVRE
GSWLQARIDP ALPQRTPLPR ADLRQRHIAL GPVAVFGASN FPLAFSVAGG DTASALAAGC
PVVVKAHSAH PGTSELVGRA IQAAVAQCGL PEGVLSLLFD AGIEIGAQLV ADARIKAVGF
TGSRAGGMAL VKIAAARREP IPVYAEMSAI NPVYLLPQAL QARAPDLGKA FVGSLTLGAG
QFCTNPGLLL AIDSPALDAF IASATQTLQA VSPAAMLTAG IGQAYAQGVQ RLAAHPKVST
LARGAAPEAG RCPAALFGTD ADAFLADEAL QAEVFGASSL LVRCKDGAQL RALSEHLEGQ
LTATVHMEAD DMALAASLLP VLERKAGRVL FNDWPTGVEV CHAMVHGGPF PATSDSRSTS
VGTLAIDRFL RPVCYQDLPA ELLPAAVADG NPLKLWRRVD GALGHD
//
