ID W7C716_9LIST Unreviewed; 225 AA.
AC W7C716;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=PCORN_12122 {ECO:0000313|EMBL:EUJ28443.1};
OS Listeria cornellensis FSL F6-0969.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265820 {ECO:0000313|EMBL:EUJ28443.1, ECO:0000313|Proteomes:UP000019254};
RN [1] {ECO:0000313|EMBL:EUJ28443.1, ECO:0000313|Proteomes:UP000019254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL F6-969 {ECO:0000313|Proteomes:UP000019254};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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:EUJ28443.1}.
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DR EMBL; AODE01000022; EUJ28443.1; -; Genomic_DNA.
DR RefSeq; WP_036080149.1; NZ_AODE01000022.1.
DR AlphaFoldDB; W7C716; -.
DR STRING; 1265820.PCORN_12122; -.
DR PATRIC; fig|1265820.5.peg.2390; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000019254; 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}.
FT DOMAIN 6..222
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 35
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 225 AA; 25482 MW; 2A84FAB88D7EAD97 CRC64;
MSYNENLQAI EDKISEAAKR SSRDVADVHL VAVTKTVDVV AMEKLYNLGI RHFGENRADV
FTEKVEAFTD KTDIVWHFIG SLQTRKVRAI LPYMHFLHSL DRKSLADEIE KRATQKIACF
LQVNISEEET KHGFNAEEAI AFVKAQNYEY VEIVGLMTMA PNTDDEQTLH HVFQGLKAVQ
LEIEKLGIPN VPCHELSMGM TNDFEVAVEE GATFIRVGRA LVEEN
//
