ID A0A0A2TJE7_9BACI Unreviewed; 385 AA.
AC A0A0A2TJE7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:KGP74568.1};
GN ORFNames=N782_00350 {ECO:0000313|EMBL:KGP74568.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP74568.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP74568.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP74568.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(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:KGP74568.1}.
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DR EMBL; AVBF01000001; KGP74568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TJE7; -.
DR STRING; 1385514.N782_00350; -.
DR eggNOG; COG0399; Bacteria.
DR Proteomes; UP000030147; Unassembled WGS sequence.
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:KGP74568.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030147};
KW Transferase {ECO:0000313|EMBL:KGP74568.1}.
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 385 AA; 42677 MW; C54157DB5633E0A8 CRC64;
MEKNSSNSKQ KLYLSSPHMG GNEQLYVQEA FDSNWIAPLG PNVNKFEEEL ANYAGVNAAS
ALSSGTAAIH LALRLLGVQE GDKVFCSTLT FVASANPIMY QAAEPIFIDS EPETWNISPV
ALKNAFDDSY KKGELPKAVI VVNLYGQSAK LDEILDICEQ YEVPVIEDAA ESLGSSYKGQ
KSGSFGHFGI YSFNGNKIIT TSGGGMLVSN DEEAIKQSRF LAAQARDNAL HYQHSTYGYN
YRMSNILAGV GRGQLEVLDL RVEQKRSIFN RYVEGLNHIE GIEFMPELEG TFSNRWLTAC
LIDREKLQVN PSDIIGALAE ENIEARPVWK PLHMQPAYEQ SMFFPHDSQI VSEDLFARGI
CLPSGTNMSV EDQNRVIEII KKVLN
//
