ID   A0A0Q4KBQ6_9SPHN        Unreviewed;       826 AA.
AC   A0A0Q4KBQ6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KQN20579.1};
GN   ORFNames=ASE86_15070 {ECO:0000313|EMBL:KQN20579.1};
OS   Sphingomonas sp. Leaf33.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN20579.1, ECO:0000313|Proteomes:UP000051455};
RN   [1] {ECO:0000313|EMBL:KQN20579.1, ECO:0000313|Proteomes:UP000051455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf33 {ECO:0000313|EMBL:KQN20579.1,
RC   ECO:0000313|Proteomes:UP000051455};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN20579.1, ECO:0000313|Proteomes:UP000051455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf33 {ECO:0000313|EMBL:KQN20579.1,
RC   ECO:0000313|Proteomes:UP000051455};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQN20579.1}.
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DR   EMBL; LMLB01000011; KQN20579.1; -; Genomic_DNA.
DR   RefSeq; WP_056427589.1; NZ_LMLB01000011.1.
DR   AlphaFoldDB; A0A0Q4KBQ6; -.
DR   STRING; 1736215.ASE86_15070; -.
DR   OrthoDB; 9768668at2; -.
DR   Proteomes; UP000051455; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR30244:SF9; PROTEIN RV3402C; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KQN20579.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051455};
KW   Transferase {ECO:0000313|EMBL:KQN20579.1}.
FT   DOMAIN          392..649
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   826 AA;  86769 MW;  08C6B8E2EFFFBC64 CRC64;
     MTKLRYPLIA PRPPRPTLLG EGLARIEAAG IYSNNGPEVC RFEAAATERL FAGRGDCVTV
     ANATLGLMLA IREAAERVGR PRCYALMPAF TFAATAQAAM WAGLTPLVCD IDPGDWSASA
     THEAELLARH GQEIAVVVPY ATFGNAIDLT RYEGYARDHG VAIVIDAAAS LGTLDDDGIG
     FGAGAPFPVV YSMQATKPFA VAEGGLIHTG DTALAAKLRT MASFGFEAPR SASLPGFNAK
     LPEVLAVMAL AKLDEIEGVS ERRAGVEAAY REALAPLGLQ TPYGKRRAMG FMSALLPPHL
     APRRAEVIAA LAERGIGAAT YFSPHLGEQP LFQRDARIEP TPVADDIGAR ILSLPATDGM
     TAADAVTIAH ALLETIGLSR ATPAQRSMPI ARLLVVGGGP AGTAMLTAAA KAGKLRDLSQ
     GLILVDRGDV LGNGRLGNYA IASDSTAQTF LSAVENNPES ALAALAGHPT ATAVGEWRDK
     LGVPLATAGP FLAATGERLA TLVSGYGGEV LKGHEALKAV RAIDGIWTVR LRRLSDGHEF
     DARAENLVVA TGGHQPLDRL VEQRVAGERL THRVGDRLLQ SDEVLALGGL DRVADLLSGK
     RSPRVAVIGG STSALTTVAL LLRSRPGIPF GAGGVTLLHR RPLRPFYHSV EAAHAEGFTD
     FGPDDICPVT GFVYRLAGFR LEARELVLRM LAVDGREPDP RVRMHRIGDD EGQALDVLDR
     ADLVIAALGY RPRVLPLEDA AGRPLALAAD RDRPMVDSYC RVLGADDAPI PGLFGIGLAA
     GFIPSGRLGG EASFSGQANG LWLWQNDVGQ LIVDAVLTGE AKALAA
//