ID A0A1G6B3A4_9GAMM Unreviewed; 237 AA.
AC A0A1G6B3A4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN02927930_00630 {ECO:0000313|EMBL:SDB15157.1};
OS Pseudidiomarina indica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1159017 {ECO:0000313|EMBL:SDB15157.1, ECO:0000313|Proteomes:UP000199626};
RN [1] {ECO:0000313|Proteomes:UP000199626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10824 {ECO:0000313|Proteomes:UP000199626};
RA Varghese N., Submissions S.;
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; FMXN01000002; SDB15157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6B3A4; -.
DR STRING; 1159017.SAMN02927930_00630; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000199626; 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.
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:UP000199626}.
FT DOMAIN 24..226
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 237 AA; 26112 MW; D020203863F80981 CRC64;
MTSIAERLTE VRMQIVEQCQ QHKRLPDSVQ LIAVSKSKPI SAIVEAFNHG QRQFGENYVQ
EAVAKVQQLQ ELPIEWHFLG PIQSNKTRDI ANHFHWVHSV DRLKIAQRLS AQRSDSQAAL
NLLIQVNIDD DAAKAGIAPA QLLDFAAQIA ALPRVQLRGL MTIPAVTTDP SQTATSFAAM
NRLFLQLKSQ YPQVDTLSIG MSADWPIAIA QGATMIRIGS ALFGAREHSP QSTGDSQ
//