ID A0A448I5Q3_MYCCI Unreviewed; 249 AA.
AC A0A448I5Q3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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 Name=yggS {ECO:0000313|EMBL:VEG47690.1};
GN ORFNames=NCTC10485_01975 {ECO:0000313|EMBL:VEG47690.1};
OS Mycolicibacterium chitae (Mycobacterium chitae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1792 {ECO:0000313|EMBL:VEG47690.1, ECO:0000313|Proteomes:UP000282551};
RN [1] {ECO:0000313|EMBL:VEG47690.1, ECO:0000313|Proteomes:UP000282551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10485 {ECO:0000313|EMBL:VEG47690.1,
RC ECO:0000313|Proteomes:UP000282551};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134355; VEG47690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448I5Q3; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000282551; Chromosome 1.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000282551}.
FT DOMAIN 56..245
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 43
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 249 AA; 26431 MW; 2297ADFE96F86BB4 CRC64;
MTESTDRRIE LANSLTLLKS RLSTVAENTG RKVEEIELLP ITKFFPAADI NILTGLGCRS
FGEARDQEAR AKIEEARRDP AWPADVRWHM VGQIQRNKAR SIATWAAVVH SVSSARVAAA
LDRGATDALA AGHRAEPLGV YVQISLDGDV SRGGVDVNAP AEVDALCAQV DAAEGLKFVG
LMGVPPLDSD PDAAFAALAA ELRRVQDGFA QRLGLSAGMT QDLEIAVKHG STCVRVGTAL
MGPRPLTSP
//