ID   Q8PE80_XANCP            Unreviewed;       509 AA.
AC   Q8PE80;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   SubName: Full=Chloroacetaldehyde dehydrogenase {ECO:0000313|EMBL:AAM39420.1};
GN   Name=aldA {ECO:0000313|EMBL:AAM39420.1};
GN   OrderedLocusNames=XCC0101 {ECO:0000313|EMBL:AAM39420.1};
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:AAM39420.1, ECO:0000313|Proteomes:UP000001010};
RN   [1] {ECO:0000313|EMBL:AAM39420.1, 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).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AE008922; AAM39420.1; -; Genomic_DNA.
DR   RefSeq; NP_635496.1; NC_003902.1.
DR   RefSeq; WP_011035359.1; NC_003902.1.
DR   AlphaFoldDB; Q8PE80; -.
DR   STRING; 190485.XCC0101; -.
DR   EnsemblBacteria; AAM39420; AAM39420; XCC0101.
DR   KEGG; xcc:XCC0101; -.
DR   PATRIC; fig|190485.4.peg.112; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_6; -.
DR   OrthoDB; 9812625at2; -.
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   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:UP000001010}.
FT   DOMAIN          30..496
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   509 AA;  55516 MW;  A707729FFF7C8C77 CRC64;
     MNALPSAKSL NTDPQSIFKP RYDNFIGGAW VAPQGGQYFD NTTPITGKVF TSIARSTAPD
     IEAALDAAHA AKEAWGKTST TDRSNVLLKI ADRIEQNLEL LAYAETWDNG KPVRETLNAD
     VPLCVDHFRY FAGAIRAQEG GISEIDSDTI AYHFHEPLGV VGQIIPWNFP LLMACWKLAP
     ALAAGNCVVM KPAEQTPASI LVLMEVIGDL LPPGVLNVVN GFGLEAGKPL ASNPRIAKIA
     FTGETTTGRL IMQYASQNLI PVTLELGGKS PNIFFADVMA EDDDFLDKAV EGFVLFAFNQ
     GEVCTCPSRA LIQESIYDTF MEKALKRVAA IKQGNPLDPN TMVGAQASSE QLEKILSYID
     IGKQEGAEIL IGGERNMLDG ELSDGFYVKP TVFKGHNKMR VFQEEIFGPV VSVTTFKDEA
     EALAIANDTL YGLGAGVWSR DASRLYRMGR AIQAGRVWTN CYHAYPAHAA FGGYKQSGIG
     RENHKMMLDH YQQTKNLLVS YSPKALGFF
//