ID F3QIN3_9BURK Unreviewed; 241 AA.
AC F3QIN3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=HMPREF9439_00783 {ECO:0000313|EMBL:EGG56429.1};
OS Parasutterella excrementihominis YIT 11859.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Parasutterella.
OX NCBI_TaxID=762966 {ECO:0000313|EMBL:EGG56429.1, ECO:0000313|Proteomes:UP000005156};
RN [1] {ECO:0000313|EMBL:EGG56429.1, ECO:0000313|Proteomes:UP000005156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11859 {ECO:0000313|EMBL:EGG56429.1,
RC ECO:0000313|Proteomes:UP000005156};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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:EGG56429.1}.
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DR EMBL; AFBP01000017; EGG56429.1; -; Genomic_DNA.
DR RefSeq; WP_008811984.1; NZ_GL883690.1.
DR AlphaFoldDB; F3QIN3; -.
DR GeneID; 43348268; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_0_1_4; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000005156; 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 37..235
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 40
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 241 AA; 27123 MW; 693CAB403DE7E802 CRC64;
MSILKPGLEE RYKRVKQSLA DDEMRFGREP GSVFLLPVSK TFGINALEEA VKCGMRAFGE
NYVQEGCEKI EYFKKQHPDL EITWHFIGHL QSNKTRPVAE HFDWVQTVDR LKIAQRLSEQ
RPADMPPLNV LIEVHISDEE SKSGCQPADV PALAQAITLL PNLKLRGIMA IPAPSDTEEG
KKAPLKEMYA IFLHLRDELN FDIDTLSMGM SSDMAEAVEC GSTMVRVGSA IFGPRDYTKK
E
//
