ID A0A0A2TJQ6_9FIRM Unreviewed; 388 AA.
AC A0A0A2TJQ6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KGP75869.1};
GN ORFNames=JT05_08075 {ECO:0000313|EMBL:KGP75869.1};
OS Desulfosporosinus sp. Tol-M.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP75869.1, ECO:0000313|Proteomes:UP000030439};
RN [1] {ECO:0000313|EMBL:KGP75869.1, ECO:0000313|Proteomes:UP000030439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abu Laban N., Tan B., Dao A., Foght J.;
RT "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT probing of toluene- degrading methanogenic culture enriched from oil sands
RT tailing of Alberta, Canada.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KGP75869.1}.
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DR EMBL; JQID01000113; KGP75869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TJQ6; -.
DR STRING; 1536651.JT05_08075; -.
DR Proteomes; UP000030439; 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; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:KGP75869.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030439};
KW Transferase {ECO:0000313|EMBL:KGP75869.1}.
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 388 AA; 43408 MW; 4A1B3A946E4CA287 CRC64;
MKKEFDPKTI IQTLQGVLPR EQKSIALHEP LFKGNEWNYV KKCLDSGWVS STGKDVDRFE
KQLAEYSGIK HVIAVVNGTA ALHICLQLAG VTSGDEVLVP ALTFIATTNA VSYCGAVPHF
ADNEERTLGL DPFKLGDYLR EISELRTEGC FNKKSGRRIK AVLPMHTFGH PVDIDPLMEV
CQRYKLMLVE DAAESLGSLY KGYHTGCWGR LSALSFNGNK IVTTGGGGAI LTNESSLAVL
ARHLTTQAKL PHAWSFNHDM VGYNYRMPNI NAALGCAQLE QLPEFIKQKR SLAVRYQEAF
ADLKGVKAFK EADFARSNYW LNVLLLDEEY SAARDTILEL TNKLGIMTRP AWTLMHQLPM
YQYCPRMDLS TAENLERRII NLPSSAFL
//
