ID   A0A1G5SEV4_9PROT        Unreviewed;       239 AA.
AC   A0A1G5SEV4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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   Name=yggS {ECO:0000313|EMBL:SCZ84949.1};
GN   ORFNames=NSMM_310031 {ECO:0000313|EMBL:SCZ84949.1};
OS   Nitrosomonas mobilis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=51642 {ECO:0000313|EMBL:SCZ84949.1, ECO:0000313|Proteomes:UP000198729};
RN   [1] {ECO:0000313|EMBL:SCZ84949.1, ECO:0000313|Proteomes:UP000198729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1 {ECO:0000313|EMBL:SCZ84949.1};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMWO01000038; SCZ84949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5SEV4; -.
DR   STRING; 51642.NSMM_310031; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000198729; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06824; PLPDE_III_Yggs_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:UP000198729}.
FT   DOMAIN          41..225
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   239 AA;  26385 MW;  196E3DC0EA781F3D CRC64;
     MTSIADRLQA VKTRIADAAK QCGRDPQTIQ LLAASKTNPP ENLRAAWEAG QTVFGENYLQ
     EGLVKIKALA DLPIEWHFIG PIQSNKTKLI AENFAWVHGI DREKIANRLS VARPDTLPPL
     QVCVQVNVSG EITKSGVDPE KVAELAAYVS ELPRLQLRGL MAVPELTAVT ALQREQFQQL
     REIFEQLKQL GFNLDTLSMG MSEDLENAVA EGATMVRIGT AIFGPRRYAI PEELGSRQQ
//