ID A3X6W6_9RHOB Unreviewed; 219 AA.
AC A3X6W6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=MED193_14637 {ECO:0000313|EMBL:EAQ46441.1};
OS Roseobacter sp. MED193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ46441.1, ECO:0000313|Proteomes:UP000005943};
RN [1] {ECO:0000313|EMBL:EAQ46441.1, ECO:0000313|Proteomes:UP000005943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ46441.1,
RC ECO:0000313|Proteomes:UP000005943};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ46441.1}.
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DR EMBL; AANB01000002; EAQ46441.1; -; Genomic_DNA.
DR RefSeq; WP_009810433.1; NZ_CH902583.1.
DR AlphaFoldDB; A3X6W6; -.
DR SMR; A3X6W6; -.
DR STRING; 314262.MED193_14637; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_1_1_5; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000005943; 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}.
FT DOMAIN 3..214
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 31
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 219 AA; 23582 MW; 76B602E70298EE71 CRC64;
MSLQEIKTRI TAAEAAADRP AGSVTLIAVS KVQPNDRVAA VLDEGQRCFG ENRVQEALGK
WPDFAETYTD LDLHLIGPLQ TNKARQAMEL FNAIHTVDRP KLAKTLARLA QELGKCPDLF
IQINTGAEPQ KAGILPAEAD DFIAECRTLD LPVKGLMCIP PVDEVAAKHF TMLAEMATRN
GLDGLSMGMS SDFEQAIAHG ATHVRVGSAI FGARAYAQA
//
