ID B2JT07_PARP8 Unreviewed; 375 AA.
AC B2JT07;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative serine-pyruvate aminotransferase {ECO:0000313|EMBL:ACC75710.1};
GN OrderedLocusNames=Bphy_6685 {ECO:0000313|EMBL:ACC75710.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OG Plasmid pBPHY01 {ECO:0000313|EMBL:ACC75710.1,
OG ECO:0000313|Proteomes:UP000001192}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC75710.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RC PLASMID=Plasmid pBPHY01 {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CP001045; ACC75710.1; -; Genomic_DNA.
DR RefSeq; WP_012405869.1; NZ_CADFGH010000024.1.
DR AlphaFoldDB; B2JT07; -.
DR KEGG; bph:Bphy_6685; -.
DR HOGENOM; CLU_044792_0_0_4; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000001192; Plasmid pBPHY01.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACC75710.1};
KW Plasmid {ECO:0000313|EMBL:ACC75710.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:ACC75710.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW Transferase {ECO:0000313|EMBL:ACC75710.1}.
FT DOMAIN 21..292
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 375 AA; 40970 MW; AE3FF7CBEA944F4A CRC64;
MPGLLPDVDR EGLLEYSVVY TDRSINHMSH LFQGVMRDIS DALKKVYNAK SVAIVPGSGT
FGMEAVARQF ATNRKCLVIR NGWFSYRWSQ IFDMGGIPSE SIVLKARPVE EGRQAAYAPA
PIEEVVAAIK ENKPDLVFAP HVETASGMML PDDYLREVAD AVHAVGGMFV LDCIASGTIW
VDMQASGVDI LISAPQKGWS ASPCCALVML SPLARERIDA TTSTSFSCDL RKWLQIMEAY
ENGGFAYHAT MPTDSLATLR DVMMETEAYG FDKVRVEQLE LGKRIRALLN DAGFKSVAAE
GFQAPGVVVS YTDDDGIRSG KKFADAGLQI APGVPLQVDE PEDFKTFRIG LFGLDKLHDV
EGSVARFAKA LNSIR
//
