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Database: UniProt
Entry: A0QU06_MYCS2
LinkDB: A0QU06_MYCS2
Original site: A0QU06_MYCS2 
ID   A0QU06_MYCS2            Unreviewed;       252 AA.
AC   A0QU06;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 106.
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   OrderedLocusNames=MSMEG_2032 {ECO:0000313|EMBL:ABK74747.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK74747.1, ECO:0000313|Proteomes:UP000000757};
RN   [1] {ECO:0000313|EMBL:ABK74747.1, ECO:0000313|Proteomes:UP000000757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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; CP000480; ABK74747.1; -; Genomic_DNA.
DR   RefSeq; WP_011728103.1; NZ_SIJM01000021.1.
DR   RefSeq; YP_886394.1; NC_008596.1.
DR   AlphaFoldDB; A0QU06; -.
DR   STRING; 246196.MSMEG_2032; -.
DR   PaxDb; 246196-MSMEI_1986; -.
DR   GeneID; 66733460; -.
DR   KEGG; msm:MSMEG_2032; -.
DR   PATRIC; fig|246196.19.peg.2007; -.
DR   eggNOG; COG0325; Bacteria.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000000757; 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.
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:UP000000757}.
FT   DOMAIN          22..242
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         50
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   252 AA;  27680 MW;  853294B6373EC298 CRC64;
     MTGSDTTAYS TARTVEDFTR NLQAVNTRIG AALQRAGREP GEVRLLPVSK TVDEDRLRVA
     AAAGCTMFGE NKVQEAMRKW RNLSDLDVEW SVIGHLQTNK AKDVAEFAAE FQALDNPRAA
     AALDRRLQAL GRQLDVYVQV NTSGEESKYG LAPDDVIPFL KTLPAYTALR VRGLMTIAVF
     STDPERVRPC FRLLRSLRDQ ARDLDLIGPG ELSMGMSGDY ELAIAEGSTC VRVGQAIFGA
     RPTPDSQYWP GN
//
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