ID A0A0Q0ZA97_9CORY Unreviewed; 231 AA.
AC A0A0Q0ZA97;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=Clow_00960 {ECO:0000313|EMBL:KQB86752.1};
OS Corynebacterium lowii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB86752.1, ECO:0000313|Proteomes:UP000050488};
RN [1] {ECO:0000313|EMBL:KQB86752.1, ECO:0000313|Proteomes:UP000050488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB86752.1,
RC ECO:0000313|Proteomes:UP000050488};
RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT human clinical disease and and emended description of Corynebacterium
RT mastiditis.";
RL Submitted (OCT-2015) 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}.
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:KQB86752.1}.
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DR EMBL; LKEV01000002; KQB86752.1; -; Genomic_DNA.
DR RefSeq; WP_055176985.1; NZ_LKEV01000002.1.
DR AlphaFoldDB; A0A0Q0ZA97; -.
DR STRING; 1544413.Clow_00960; -.
DR PATRIC; fig|1544413.3.peg.964; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000050488; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050488}.
FT DOMAIN 10..229
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 231 AA; 25094 MW; 1C2DD794DB43099E CRC64;
MSRIEELRGN LAAVREHIAA CAREAGRDPQ EITLLPVTKF HPASDIALLA DLGVTEVGEN
REQEARAKAQ EIPQMRFHMI GQVQTKKANH VARWAASVHS VDSLKLIEAL NRGAGRALES
GERTEVLPCF IQWSADGDTQ RGGSTQPAEL IDALVAAEHL RPAGIMCVPP LGSDPAEIFR
RAHHLRVEEE ERLGQRLLLS AGMSGDMREA IAAGTDIVRV GTRIMGARPL A
//