ID D8FKG6_9FIRM Unreviewed; 228 AA.
AC D8FKG6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=HMPREF9131_0993 {ECO:0000313|EMBL:EFK38429.1};
OS Peptoniphilus sp. oral taxon 836 str. F0141.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=768724 {ECO:0000313|EMBL:EFK38429.1, ECO:0000313|Proteomes:UP000004869};
RN [1] {ECO:0000313|EMBL:EFK38429.1, ECO:0000313|Proteomes:UP000004869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0141 {ECO:0000313|EMBL:EFK38429.1,
RC ECO:0000313|Proteomes:UP000004869};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.;
RT "Genome Sequence of Peptoniphilus sp. oral taxon 836 str. F0141.";
RL Submitted (JUN-2010) 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:EFK38429.1}.
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DR EMBL; AEAA01000122; EFK38429.1; -; Genomic_DNA.
DR RefSeq; WP_009346110.1; NZ_AEAA01000122.1.
DR AlphaFoldDB; D8FKG6; -.
DR Proteomes; UP000004869; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW ECO:0000256|PIRSR:PIRSR004848-1}.
FT DOMAIN 13..224
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 228 AA; 26340 MW; C09B80E939F69D94 CRC64;
MSVKDNLKFV MEEIEKAKRH SLTNEDVNLI AVTKNHETDV IKEAIDLGIT DIGENRVQEL
KSKIDELGPI VNYHMIGNLQ TNKVKYIYNR VYMIQSLDTL KLAKEIDKRA GSDGIEVNCL
IQINIGNEEQ KSGIAYEDTL KFIYNLMDFK HISIRGLMAI APNTDDKQYL RRLFRKMFEM
KEKIIKENIS SVRMDYLSMG MSSDYQIAIE EGSNMVRIGT KIFGKRIY
//
