ID A0A0S8F0Q5_9GAMM Unreviewed; 229 AA.
AC A0A0S8F0Q5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=AMS22_05955 {ECO:0000313|EMBL:KPK54389.1};
OS Thiotrichales bacterium SG8_50.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX NCBI_TaxID=1703416 {ECO:0000313|EMBL:KPK54389.1, ECO:0000313|Proteomes:UP000051903};
RN [1] {ECO:0000313|EMBL:KPK54389.1, ECO:0000313|Proteomes:UP000051903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_50 {ECO:0000313|EMBL:KPK54389.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK54389.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJTW01000053; KPK54389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8F0Q5; -.
DR PATRIC; fig|1703416.3.peg.2943; -.
DR Proteomes; UP000051903; 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}.
FT DOMAIN 8..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 229 AA; 24824 MW; E6363D7A5F3419F1 CRC64;
MSTIAARLQA VRARIRAAEA ASGRPPDVVR LIAVSKTFAA SAVREACQAG QHAFGENYLQ
EALSKIEALP GLPLEWHFIG PIQSNKARPV AQHFAWVHTV DRLKLAERLS AARPDGLPPL
QVCIQVNVSG ERTKSGCDPD SLEELALAVA NLPRLQLRGL MAIPEPTSDL DLQRQRFGLL
RHLKDQLVSS GLSLDALSMG MSDDLEQAIA EGATMVRVGR AIFGQRQAR
//