ID A0A2V4BBV9_9PSEU Unreviewed; 376 AA.
AC A0A2V4BBV9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:PXY32750.1};
GN ORFNames=BAY60_05730 {ECO:0000313|EMBL:PXY32750.1};
OS Prauserella muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=588067 {ECO:0000313|EMBL:PXY32750.1, ECO:0000313|Proteomes:UP000249915};
RN [1] {ECO:0000313|EMBL:PXY32750.1, ECO:0000313|Proteomes:UP000249915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45305 {ECO:0000313|EMBL:PXY32750.1,
RC ECO:0000313|Proteomes:UP000249915};
RA Ruckert C., Albersmeier A., Jiang C.-L., Jiang Y., Kalinowski J.,
RA Schneider O., Winkler A., Zotchev S.B.;
RT "Draft genome sequence of Prauserella muralis DSM 45305, isolated from a
RT mould-covered wall in an indoor environment.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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|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:PXY32750.1}.
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DR EMBL; MASW01000001; PXY32750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4BBV9; -.
DR Proteomes; UP000249915; 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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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:PXY32750.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000249915};
KW Transferase {ECO:0000313|EMBL:PXY32750.1}.
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 180
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 376 AA; 39481 MW; B898CFDDCA59DA88 CRC64;
MALGQPTVGD EELAAVAEVL RSGWLAGAGP ACAEFERRFA TAVGTGHALA TANCGSALQL
GLTVLGVRPG DEVIVGDYTF PATGHAVLHA GATPVFADVS PDTWCADPAA IETLVGPRTV
GILAVDVAGQ PGDFDAYRAI ADRHGLWLFE DAACSAGATY RARPAGSLAD LAAFSFHGRK
GITAGEGGAL VGDRADLIEH ARRLHSYGIE PAISREGAEG LPIPVFSEAG HNFRMSEVQA
AIMTVQLDRL PALLAARRAV AKRYHEAFAD LDGVEPPAEL PDREHAWQSY LLTIDPALGR
DAVALYLRER GVQCTFGTYA SHLQPVYGPQ PSLPVSARAF ASQVAIPLHA NLTEQQVDRV
IATVRDAVAA SGRTQE
//