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Database: UniProt
Entry: A0A2R7RDF7_9MICC
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ID   A0A2R7RDF7_9MICC        Unreviewed;       329 AA.
AC   A0A2R7RDF7;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:PTT68968.1};
DE   Flags: Fragment;
GN   ORFNames=DBR22_05130 {ECO:0000313|EMBL:PTT68968.1};
OS   Arthrobacter sp. HMWF013.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=2056849 {ECO:0000313|EMBL:PTT68968.1, ECO:0000313|Proteomes:UP000244718};
RN   [1] {ECO:0000313|EMBL:PTT68968.1, ECO:0000313|Proteomes:UP000244718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMWF013 {ECO:0000313|EMBL:PTT68968.1,
RC   ECO:0000313|Proteomes:UP000244718};
RA   Go L.Y., Mitchell J.A.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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:PTT68968.1}.
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DR   EMBL; QAIQ01000107; PTT68968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R7RDF7; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000244718; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; 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; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:PTT68968.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244718};
KW   Transferase {ECO:0000313|EMBL:PTT68968.1}.
FT   MOD_RES         156
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PTT68968.1"
SQ   SEQUENCE   329 AA;  34765 MW;  EE185812B843A9CA CRC64;
     FTTGATMANF TGLAAARWRL LADAGWNLDR YGLAGAPRIR CFVGQERHDT IDMGLRYLGL
     GSPTLVPTDD QGRLLADPLD TMLSEGPGPA IVCLQAGNLH SGAFDPFENA IRIARRHGAW
     VHVDGAFGLW AAAVPELAGL TAGMAQADSW GTDAHKTLNV PYDCGIAIVR DTGALRGAMG
     LATTSYMVHD AEGPGDPFQK VPELSRRGRG ITVWAALRSL GREGVAAQVR GLAGAAARIS
     RRLAEVEGIE VLNDVDYTQV SLAFGDDAIT RAVAARLIED GKVWMSGSHW QGRDVLRVSV
     SNWSTDADDV DTAVEAVSSA FAAVKSAGN
//
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