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Database: UniProt
Entry: A0A1Z2L8C8_9ACTN
LinkDB: A0A1Z2L8C8_9ACTN
Original site: A0A1Z2L8C8_9ACTN 
ID   A0A1Z2L8C8_9ACTN        Unreviewed;       225 AA.
AC   A0A1Z2L8C8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
DE            Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
GN   ORFNames=SMD11_4974 {ECO:0000313|EMBL:ARZ70567.1};
OS   Streptomyces albireticuli.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ70567.1, ECO:0000313|Proteomes:UP000195755};
RN   [1] {ECO:0000313|EMBL:ARZ70567.1, ECO:0000313|Proteomes:UP000195755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ70567.1,
RC   ECO:0000313|Proteomes:UP000195755};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT   "Streptomyces albireticuli Genome sequencing and assembly.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC       involved in PLP homeostasis. {ECO:0000256|HAMAP-Rule:MF_02087}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004848-1};
CC   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_02087,
CC       ECO:0000256|RuleBase:RU004514}.
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DR   EMBL; CP021744; ARZ70567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z2L8C8; -.
DR   KEGG; salj:SMD11_4974; -.
DR   Proteomes; UP000195755; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00635; PLPDE_III_YBL036c_like; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_02087; PLP_homeostasis; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR011078; PyrdxlP_homeostasis.
DR   NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR   PANTHER; PTHR10146; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1.
DR   PANTHER; PTHR10146:SF14; PYRIDOXAL PHOSPHATE HOMEOSTASIS PROTEIN; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS01211; UPF0001; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1}.
FT   DOMAIN          15..222
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         26
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   225 AA;  23217 MW;  01346018508870D0 CRC64;
     MEERISSACA AAGRARDEVT LIVVTKIYPA SDVRLLAELG VRHVAENRDQ DAAPKAAECA
     DLPLTWHFVG QLQTNKVRSV VSYADVVHSV DRDRLVTALS AAAVRAGREL DCLIQVALDA
     ESGERGDRGG VAPDGVAALA DGLAAAEGLR PAGLMTVAPL AGPFAGRPRA AFDRLLEIST
     GMRAAHPAAN MVSAGMSADL DDAVAAGATH VRVGSAVLGV RPRLG
//
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