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Database: UniProt
Entry: A0A124FN56_9CHLR
LinkDB: A0A124FN56_9CHLR
Original site: A0A124FN56_9CHLR 
ID   A0A124FN56_9CHLR        Unreviewed;       394 AA.
AC   A0A124FN56;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:KUK46856.1};
GN   ORFNames=XD73_0260 {ECO:0000313|EMBL:KUK46856.1};
OS   Anaerolinea thermophila.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Anaerolinea.
OX   NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK46856.1, ECO:0000313|Proteomes:UP000064249};
RN   [1] {ECO:0000313|EMBL:KUK46856.1, ECO:0000313|Proteomes:UP000064249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=46_16 {ECO:0000313|EMBL:KUK46856.1};
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {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:KUK46856.1}.
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DR   EMBL; LGFU01000005; KUK46856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124FN56; -.
DR   PATRIC; fig|167964.4.peg.95; -.
DR   Proteomes; UP000064249; Unassembled WGS sequence.
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:KUK46856.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KUK46856.1}.
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   394 AA;  43794 MW;  AA914119B3E93451 CRC64;
     MTKRQEKSVP MSSPEINEED RQAVLEVLDT RYLSMGPKIE QFEQTIREFT GSQYAIAVNS
     GTAGLHLCIR AAGVEQGDIV ITTPFSFISS TNVILFEKAI PVFVDIDPIS GNMDPKQVEQ
     AINDLKNGGA AAAKWIPRRG GEKPGAVKAV LSVDVFGQPA DYDPIEKICE KNNLALIEDS
     CEALGATYKG RKAGTLGTYG VFAFYPNKQI TTGEGGIIIT DDEKAAAFMQ ALRNQGRAPG
     DAWLQHTYLG YNYRLDEMSA ALGLSQLKRL DHMLQTRAQV AQWYETYLQE FDLIQTPHIL
     PTTTQMSWFV YVIRVDASLD RDEFARRMIA NGIPVRPYFL PIHLQPYLME QFGYQPGDYP
     VSEDLGNRGL ALPFSSVMSE EQVMAVCEGI RKSL
//
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