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Database: UniProt/TrEMBL
Entry: U4LXU7_9XANT
LinkDB: U4LXU7_9XANT
Original site: U4LXU7_9XANT 
ID   U4LXU7_9XANT            Unreviewed;       489 AA.
AC   U4LXU7; A0A099QD01;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   28-MAR-2018, entry version 27.
DE   SubName: Full=Putative aldehyde dehydrogenase {ECO:0000313|EMBL:CDF60516.1};
GN   ORFNames=XFF4834R_chr08850 {ECO:0000313|EMBL:CDF60516.1};
OS   Xanthomonas fuscans subsp. fuscans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=366649 {ECO:0000313|EMBL:CDF60516.1, ECO:0000313|Proteomes:UP000016941};
RN   [1] {ECO:0000313|EMBL:CDF60516.1, ECO:0000313|Proteomes:UP000016941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4834-R {ECO:0000313|EMBL:CDF60516.1,
RC   ECO:0000313|Proteomes:UP000016941};
RX   PubMed=24195767; DOI=10.1186/1471-2164-14-761;
RA   Darrasse A., Carrare S., Barbe V., Boureau T., Arrieta-Ortiz M.L.,
RA   Bonneau S., Briand M., Brin C., Cociancich S., Durand K., Fouteau S.,
RA   Gagnevin L., Guarin F., Guy E., Indiana A., Koebnik R., Lauber E.,
RA   Munoz A., No.l L.D., Pieretti I., Poussier S., Pruvost O.,
RA   Rob.ne-Soustrade I., Rott P., Royer M., Serres-Giardi L., Szurek B.,
RA   van Sluys M.A., Verdier V., Verniere C., Arlat M., Manceau C.,
RA   Jacques M.A.;
RT   "Genome sequence of Xanthomonas fuscans subsp. fuscans strain 4834-R
RT   reveals that flagellar motility is not a general feature of
RT   xanthomonads.";
RL   BMC Genomics 14:761-761(2013).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; FO681494; CDF60516.1; -; Genomic_DNA.
DR   RefSeq; WP_022558372.1; NZ_CP023294.1.
DR   EnsemblBacteria; CDF60516; CDF60516; XFF4834R_chr08850.
DR   EnsemblBacteria; KGK65671; KGK65671; NB99_12855.
DR   KEGG; xfu:XFF4834R_chr08850; -.
DR   PATRIC; fig|1240239.3.peg.945; -.
DR   KO; K00128; -.
DR   Proteomes; UP000016941; 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   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000016941};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345}.
SQ   SEQUENCE   489 AA;  52420 MW;  35F71EF243DA7A69 CRC64;
     MEALSETLRG IAARSPLGLF IDGQWRASTG DRTVDVIAPH TEERLLCYTE PSQADTEAAI
     AAARSAFDNG PWPQLSPQER SVVLKRVADH LRARMPELAE AWTGQVGATL GFSKRASQQA
     PDLFDYYADL IATHAFVEPR VRPNGGRVHV VQEPVGVVAA ITPWNAPLVL LCYKVAAALA
     AGCTVVAKPS PETPIDAYIL AECISAAGVP DGVFNLLPAG REVGEQLIRH PHVDKVSFTG
     STQAGRSIGI ACAERLARVG LELGGKSAAI VLEDADLAKM LPTLVPYSMP IAGQVCFSLT
     RILVPTQRRE EILQAYCTAL GAVKLGDPFA ADTGMGPLAL GRQLERVQSY IAKGKAEGAR
     LVMGGSRPAH LSRGFFVEPT VFAEVTPDMA IAREEIFGPV VSFIDYHDEA DLIAKANASD
     YGLHGTIYSE DAERAYRIAR RVRSGSHAIN GMWVDISMPF GGFKHSGIGR EGGIEGLHAF
     LETRTLYLS
//
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