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Database: UniProt
Entry: A0A0A7PKI3_9SPHN
LinkDB: A0A0A7PKI3_9SPHN
Original site: A0A0A7PKI3_9SPHN 
ID   A0A0A7PKI3_9SPHN        Unreviewed;       332 AA.
AC   A0A0A7PKI3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:AJA09698.1};
GN   ORFNames=SKP52_14065 {ECO:0000313|EMBL:AJA09698.1};
OS   Sphingopyxis fribergensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA09698.1, ECO:0000313|Proteomes:UP000030907};
RN   [1] {ECO:0000313|EMBL:AJA09698.1, ECO:0000313|Proteomes:UP000030907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA09698.1,
RC   ECO:0000313|Proteomes:UP000030907};
RX   PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA   Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA   Tischler D.;
RT   "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT   the ability to degrade styrene and phenylacetic acid.";
RL   Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP009122; AJA09698.1; -; Genomic_DNA.
DR   RefSeq; WP_039575608.1; NZ_CP009122.1.
DR   AlphaFoldDB; A0A0A7PKI3; -.
DR   STRING; 1515612.SKP52_14065; -.
DR   KEGG; sphk:SKP52_14065; -.
DR   HOGENOM; CLU_033332_0_1_5; -.
DR   OrthoDB; 9768668at2; -.
DR   Proteomes; UP000030907; 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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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:AJA09698.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW   Transferase {ECO:0000313|EMBL:AJA09698.1}.
SQ   SEQUENCE   332 AA;  37525 MW;  3427E71A75D32457 CRC64;
     MSGDIAHPSP LPFSVAFDPR DEDEVIRRWR GLLRGNHWSH GAELEEFEAT WKAWNELPAI
     GFDNWAGAAA AILDFFQVAG KTVLCPSNTF LATPRSALRA GASVEFYDCN REDLCGSYTD
     FVEKAERHKP ALAYIVHIGG HIAFDIHRIA EYCRANQIAL IEDCAHAVGA EWNGVKPGAF
     GDAGIFSLYA TKTISTGEGG VAVTANPDLE RHVRSFRDYG RGSRYKIQGM NHRLDEFRAA
     LGVVQMRRMP EIVSWKQRYA REVLDLRYPN RVQMPNGMES GYYKYIVFDE IPQTTGRVYE
     LPCHEIFDSS ISLPNTEWAT NNHWCVPIYY PK
//
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