ID A0A3P1Y4Q0_9BACT Unreviewed; 395 AA.
AC A0A3P1Y4Q0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RRD65136.1};
GN ORFNames=EII26_04495 {ECO:0000313|EMBL:RRD65136.1};
OS Fretibacterium sp. OH1220_COT-178.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=2491047 {ECO:0000313|EMBL:RRD65136.1, ECO:0000313|Proteomes:UP000267192};
RN [1] {ECO:0000313|EMBL:RRD65136.1, ECO:0000313|Proteomes:UP000267192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1220_COT-178 {ECO:0000313|EMBL:RRD65136.1,
RC ECO:0000313|Proteomes:UP000267192};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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:RRD65136.1}.
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DR EMBL; RQYL01000007; RRD65136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1Y4Q0; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000267192; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:RRD65136.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000267192};
KW Transferase {ECO:0000313|EMBL:RRD65136.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 395 AA; 42253 MW; AAA72B7220341BC8 CRC64;
MSHAAQGFGT KCVHFGTCPD PVTGALNTPI YQTSTFAFED ADQGARRFAG EEEGYIYTRL
GNPNHTAVER KLAALEGGEA AAVASSGMGA IASVLWTALS GGDHVIAANS IYGCTHSLMN
HHFPRFGIEV TFMSLADLAA VKAAVKPNTR VIYCESPANP TMEIADLEGL AKIAHEAGAL
LIVDNTYCSP VIQRPIEFGA DVVLHSVTKY LNGHGDVIAG AAVGSAEFIA RVKGEGLKDL
TGATMSPFDA YLMLRGMKTL HVRVPRHCET ALEIARFLEK RPEVAHVWYP GLDSFPQKEL
ARKQMKYFGA MIAMDLKGGF EAGKKFINST KLWTLAVSLG DTESLIQHPA SMTHSALSDE
EQAAAGISKG LIRLSVGLED AEDLKADLDR AFSAL
//
