ID E3CCT3_STRPA Unreviewed; 222 AA.
AC E3CCT3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=HMPREF9626_1482 {ECO:0000313|EMBL:EFQ55446.1};
OS Streptococcus parasanguinis F0405.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=905067 {ECO:0000313|EMBL:EFQ55446.1, ECO:0000313|Proteomes:UP000003812};
RN [1] {ECO:0000313|EMBL:EFQ55446.1, ECO:0000313|Proteomes:UP000003812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0405 {ECO:0000313|EMBL:EFQ55446.1,
RC ECO:0000313|Proteomes:UP000003812};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-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:EFQ55446.1}.
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DR EMBL; AEKM01000006; EFQ55446.1; -; Genomic_DNA.
DR RefSeq; WP_003002475.1; NZ_AEKM01000006.1.
DR AlphaFoldDB; E3CCT3; -.
DR Proteomes; UP000003812; 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 8..221
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 222 AA; 25367 MW; D8B7FDE2202BD2C8 CRC64;
MNLVENADLV RQQVETARNK ANRQDQVNVI AVTKYVDVTT TEALVKTGIQ HIGENRVDKF
LEKYQALKEY DLTWHLIGSL QRRKVKDVIN LVDYFHALDS VKLAQEIQKR AEHPIKCFLQ
VNISGEESKH GFAPDELDDV LAEIAQLDKI EIVGLMTMAP FEASQEELQD IFSKTHQLQK
QLEKKQLKNM PFSELSMGMS RDFEVAIANG ATYVRIGTSF FK
//
