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Database: UniProt
Entry: A0A3M2LGW8_9ACTN
LinkDB: A0A3M2LGW8_9ACTN
Original site: A0A3M2LGW8_9ACTN 
ID   A0A3M2LGW8_9ACTN        Unreviewed;       377 AA.
AC   A0A3M2LGW8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Pyridoxal-phosphate dependent enzyme {ECO:0000313|EMBL:RMI36757.1};
GN   ORFNames=EBN88_20725 {ECO:0000313|EMBL:RMI36757.1};
OS   Streptomyces triticirhizae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2483353 {ECO:0000313|EMBL:RMI36757.1, ECO:0000313|Proteomes:UP000278673};
RN   [1] {ECO:0000313|EMBL:RMI36757.1, ECO:0000313|Proteomes:UP000278673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY642 {ECO:0000313|EMBL:RMI36757.1,
RC   ECO:0000313|Proteomes:UP000278673};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of actinobacteria from
RT   wheat.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:RMI36757.1}.
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DR   EMBL; RFFJ01000133; RMI36757.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2LGW8; -.
DR   Proteomes; UP000278673; Unassembled WGS sequence.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          71..316
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  40692 MW;  696E2F7C7E1D91BB CRC64;
     MPTNVPANAP TNAPTNAPAN VPAPGTPAQP PPKQAPLRPP VIHEHITDAV KAPDLVRLGP
     GVVLARFETL KVYAALGAVR TLLERGVIRR GQTLVDSSSG IYALALAMAC HRYGLRCHIV
     ASTTVDLTTR VQLEILGATI DQMPPSDDLR LDQNRRVARV RELVAARPEA HWMRQYHDAV
     HYAGYREFAD LVAAALPDGP LTVVAPVGTG SSSGGLVVPL RQRGLDARLV GVQPFGSVTF
     GSERFRDPEA IIAGIGSAIP FENVRHRLYD GLHWVDFRHA LAGAVGLVRS HAVFAGLSTG
     AAHLAALWEA GRRPERTHLV IGADTGHRYA ERAFARHREA PDPRSLKPHQ ITELADLTPP
     WSAMEWGRRP YEPAGTA
//
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