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Database: UniProt
Entry: A9BQS7_DELAS
LinkDB: A9BQS7_DELAS
Original site: A9BQS7_DELAS 
ID   A9BQS7_DELAS            Unreviewed;       408 AA.
AC   A9BQS7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ABX32779.1};
GN   OrderedLocusNames=Daci_0133 {ECO:0000313|EMBL:ABX32779.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX32779.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX32779.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP000884; ABX32779.1; -; Genomic_DNA.
DR   RefSeq; WP_012202072.1; NC_010002.1.
DR   AlphaFoldDB; A9BQS7; -.
DR   STRING; 398578.Daci_0133; -.
DR   GeneID; 24119609; -.
DR   KEGG; dac:Daci_0133; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_036177_0_0_4; -.
DR   Proteomes; UP000000784; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABX32779.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW   Transferase {ECO:0000313|EMBL:ABX32779.1}.
SQ   SEQUENCE   408 AA;  44113 MW;  E350CBAF160DF9B0 CRC64;
     MAERVLPPTA GLPLRAADLL PWGDADLATA LAQWLGVPAV QLECSGTSAL MVALQTLRRL
     APGRSEVIAP AYTCPLVALA VAHCGLQLRL CDLHPDTLDM DPARLRSLCS ECTLAVLPTH
     LCGRVADVAT AVDCARAVGA WVVEDAAQAL GARLRGEPVG WQGDVGFYSL AVGKGLTTFE
     GGVLLARDPA LREALRETHA ASVRQDRGWE LRRSLELLGY AALYRPAGLD LAYGRPLRAA
     LSRSDWVQAA GDDFDDAIPC HELGAWRRRV GRRALARLAD FQQQLQRQAR ERGAWLSAID
     GIEVVGDTVP GAQGVWPVLL LRLRDAATRD ALLRAQWGLG WGLSLPFVHV LPDYGRYDHV
     LGLARQDVVD QGRDWAQRLV AVGNSLWFDD ARFEALLSLL EGPHAAPG
//
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