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Database: UniProt
Entry: U7UCX1_9FIRM
LinkDB: U7UCX1_9FIRM
Original site: U7UCX1_9FIRM 
ID   U7UCX1_9FIRM            Unreviewed;       230 AA.
AC   U7UCX1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=HMPREF1253_1517 {ECO:0000313|EMBL:ERT56724.1};
OS   Peptoniphilus sp. BV3C26.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=1111134 {ECO:0000313|EMBL:ERT56724.1, ECO:0000313|Proteomes:UP000017105};
RN   [1] {ECO:0000313|EMBL:ERT56724.1, ECO:0000313|Proteomes:UP000017105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3C26 {ECO:0000313|EMBL:ERT56724.1,
RC   ECO:0000313|Proteomes:UP000017105};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) 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:ERT56724.1}.
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DR   EMBL; AWXB01000065; ERT56724.1; -; Genomic_DNA.
DR   RefSeq; WP_023056361.1; NZ_AWXB01000065.1.
DR   AlphaFoldDB; U7UCX1; -.
DR   STRING; 1111134.HMPREF1253_1517; -.
DR   PATRIC; fig|1111134.3.peg.1716; -.
DR   eggNOG; COG0325; Bacteria.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000017105; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017105}.
FT   DOMAIN          6..226
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   230 AA;  26180 MW;  EFD6A0932E6D1AA5 CRC64;
     MDIKKNLEEV LNNIELAEKR SVTGEKVKLI AVTKTHGIDI IEKAIELGVK DIGENKVQEL
     TKKIEVLKDK VNYHMIGNLQ SNKVKFIYNK VKLIHSLDRL SLAKEIEKRA SQDDIKVNCL
     IQINIGDEST KGGIELRDTE KFVESLLEFN HIKIMGLMAI APDTDDEKLL RTCFKNMFNI
     KEKIKSKGYE GLEMKYLSMG MSNDYEIAIE EGANMVRVGS KIFGARNYNI
//
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