ID A0A3D8K5H2_9BURK Unreviewed; 392 AA.
AC A0A3D8K5H2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RDV00471.1};
GN ORFNames=DWV00_01390 {ECO:0000313|EMBL:RDV00471.1};
OS Trinickia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2291023 {ECO:0000313|EMBL:RDV00471.1, ECO:0000313|Proteomes:UP000256838};
RN [1] {ECO:0000313|EMBL:RDV00471.1, ECO:0000313|Proteomes:UP000256838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOM06 {ECO:0000313|EMBL:RDV00471.1,
RC ECO:0000313|Proteomes:UP000256838};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOM06 isolated from forest soil.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000256|ARBA:ARBA00001535};
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|ARBA:ARBA00009077, 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:RDV00471.1}.
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DR EMBL; QRGA01000001; RDV00471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8K5H2; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000256838; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
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 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; IPR006233; Cys_b_lyase_bac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 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:RDV00471.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000256838};
KW Transferase {ECO:0000313|EMBL:RDV00471.1}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 42481 MW; DC9B2F30E35918FA CRC64;
MPKNLSTKLI HDDYFPPVGY QAVPPGVFKG STVLFPDAVT VRERMRAFGR RDGYSYGLYG
TPTTYILEQR LCALEGARHC LLGPSGQAAI ALVNLGLLAA GDELLLPSNV YGPALRHART
TLPPLGITHQ CYDPMDPADL ERKLGPRTKL VWMEAPGSIT MEFPDLRKLV AIAKENGVVV
ALDNTWGAGV AFKPFELGVD ISIHALTKYP SGGADVLMGS VTTNDDALHE RLRIAYLDLG
MGVGANDVEF VLRGLPTLEA RYHLHDASAR SLATWMASQP AIGQVLHPAL DSCPGHEHWA
SHCSLAAGLF SVLFKSGYAS SQVDSFCDRL KLFGIGLSWG GPMSLVMPYD LPSIRSGKGC
YEGHLVRFSI GLENTDDLRE DLEQAMKASF GR
//
