ID A0A0G0PAH9_9BACT Unreviewed; 451 AA.
AC A0A0G0PAH9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:KKQ86316.1};
GN ORFNames=UT09_C0038G0005 {ECO:0000313|EMBL:KKQ86316.1};
OS Parcubacteria group bacterium GW2011_GWF2_38_8.
OC Bacteria.
OX NCBI_TaxID=1618961 {ECO:0000313|EMBL:KKQ86316.1, ECO:0000313|Proteomes:UP000034262};
RN [1] {ECO:0000313|EMBL:KKQ86316.1, ECO:0000313|Proteomes:UP000034262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ86316.1}.
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DR EMBL; LBVM01000038; KKQ86316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0PAH9; -.
DR Proteomes; UP000034262; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 2.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KKQ86316.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:KKQ86316.1}.
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 451 AA; 51212 MW; 6022ED9C3FE26DA0 CRC64;
MLDRSLCSLV IIVGIEIKNN PTTLTSLTIL TTIMIFTSLS PNTEADDIFL ALKILISPWL
WVKGRAVKEL ENTFKQWLGV KYVFAFSSGR TCLYVILSSL GLSKNDEVLL QAYTCVAVPN
SIIWAGAKPV YVDCEETIFN MSVEDLKKKI TPKSKALIIQ HTFGRPTKID QLMAAAKENN
LFVIEDCAHS LGAEYQEKKV GTFGDASFFS FGRDKVISSV FGGLLTTNNR ELAEKIEARQ
NSFEYPSRLW VMRQLLHPPV MALVKLTYNF FYLGKIFLEV LKRLSIISRA VEPTEKEGGR
PPFVLKKMPN GLALLALYQF QKLDRFNAHR RKIAKLYDKE LKQLDIILPQ EKKDSFRIYL
RYPIQVNNPK MILRAAKKEG IELGDWYSSP IAPQGVNYEK VFYKLGSCPV AEKLSGQSLN
LPTHIQIKEK DALRIIKFFR SANVKTPDIL I
//
