ID T1ZGN9_STRIT Unreviewed; 419 AA.
AC T1ZGN9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:AGU77113.1};
GN ORFNames=SIR_1782 {ECO:0000313|EMBL:AGU77113.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU77113.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU77113.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU77113.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
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}.
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DR EMBL; CP003857; AGU77113.1; -; Genomic_DNA.
DR AlphaFoldDB; T1ZGN9; -.
DR KEGG; sib:SIR_1782; -.
DR PATRIC; fig|862967.3.peg.1799; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_9; -.
DR Proteomes; UP000016233; 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: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:AGU77113.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000016233};
KW Transferase {ECO:0000313|EMBL:AGU77113.1}.
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 419 AA; 47089 MW; 18EF984DBFAA7025 CRC64;
MIMDFKPFEE KIWLSSPTMH GDELKYMTEA YNTNWMSTVG QNINEVESSI CKKVGCKYAV
ALASGTSALH MAIKAAGIKH GDKVFCSTVT FGATINPIVY EGAIPVFIDS EYDTWNMDPA
ALERAFEVYP EVKVVVLVHL YGVPAKIDEI RSICEKYQAI VIEDAAESLG ASYKGIQTGS
FGAYNAISFN GNKIITGSSG GMFLTDDLEA ANKVRKWSTQ ARENAPWYQH EEIGYNYRMS
NVIAGVIRGQ SPYLEEHIAQ KKAIYQRYKE GLKDLPISMN PYDEKKSEPN FWLSCLLIDE
QAMCKQVRGE KESLYISEEG KSCPTEILET LGRYNIEGRP IWKPMHMQPI YRNHDFITRE
GNGRARTNAY IVGGDKGEDG LPLDTGMDLF CRGLCLPSDN KMTVEQQDVI IEIIKKCFN
//
