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Database: UniProt
Entry: A0A1X9YJS3_9SPHN
LinkDB: A0A1X9YJS3_9SPHN
Original site: A0A1X9YJS3_9SPHN 
ID   A0A1X9YJS3_9SPHN        Unreviewed;       414 AA.
AC   A0A1X9YJS3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:ARS28997.1};
GN   ORFNames=KC8_17140 {ECO:0000313|EMBL:ARS28997.1};
OS   Sphingomonas sp. KC8.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS28997.1, ECO:0000313|Proteomes:UP000194475};
RN   [1] {ECO:0000313|EMBL:ARS28997.1, ECO:0000313|Proteomes:UP000194475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KC8 {ECO:0000313|EMBL:ARS28997.1};
RA   Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA   Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT   "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT   estrogens in aquatic ecosystems.";
RL   Submitted (JUN-2016) 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; CP016306; ARS28997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X9YJS3; -.
DR   STRING; 1030157.GCA_000214335_01788; -.
DR   KEGG; spkc:KC8_17140; -.
DR   eggNOG; COG0399; Bacteria.
DR   OrthoDB; 9768668at2; -.
DR   Proteomes; UP000194475; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ARS28997.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194475};
KW   Transferase {ECO:0000313|EMBL:ARS28997.1}.
FT   ACT_SITE        209
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   414 AA;  44443 MW;  C57B04FE8593BC57 CRC64;
     MPSPALTHPT LAHDRDAPKT VHFAPAVIHS RWPTHDEDEI AAVVDVLRSG RVNALCHGDR
     CRTFEQSFAA MCAMPHALSV SNGTVALELA LRVLGIDAGD EVIVTARSFV ASASCVITCG
     AKPVFADVDP VSQNLTAQSI AAVLTPRTRA IIVVHLGGFP AAMDEIMVLA EAYGLKVIED
     CAQAHGARFH GQPVGSFGDV AAFSFCTDKI MSTGGEGGML VLRTRAQWEK AWSLSNHGKD
     FTKAHLPGGG AFRWIHDDFG SNCRMTEMQA AIGSIQLAKL PGWTATRRRN AGILLETLGG
     LLNLRLVQPP GECDHAYYAF YAFTPTDPPH SAAFRDRIVA QMNDAGMPCQ SGSCPEIYRE
     QAFLAAGHTP KQSLPIARQL GQTSIKLPVD QTLAPREMQE IGRTLAGILK AECE
//
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