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Database: UniProt
Entry: A0A2V4BBV9_9PSEU
LinkDB: A0A2V4BBV9_9PSEU
Original site: A0A2V4BBV9_9PSEU 
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
//
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