ID A0A0M2RX02_9ACTN Unreviewed; 248 AA.
AC A0A0M2RX02;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=LQ51_20185 {ECO:0000313|EMBL:KKK02435.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKK02435.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKK02435.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKK02435.1,
RC ECO:0000313|Proteomes:UP000034330};
RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT National park, Assam, India.";
RL Submitted (NOV-2014) 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:KKK02435.1}.
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DR EMBL; JTGL01000163; KKK02435.1; -; Genomic_DNA.
DR RefSeq; WP_046569761.1; NZ_KQ058874.1.
DR AlphaFoldDB; A0A0M2RX02; -.
DR STRING; 1538294.LQ51_20185; -.
DR PATRIC; fig|1538294.3.peg.5273; -.
DR HOGENOM; CLU_059988_0_0_11; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000034330; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
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 29..245
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 248 AA; 25434 MW; 7C70A46746E9458F CRC64;
MTDIPGAVRP DRRAELAAGL TQVRARIADA CAAAGRDRGE VTLIAVTKTY PAGDVVALTG
LGVTDVGENR DQEAAPKAAE AAAAGAAPRW HFIGQLQRNK ARSVVRYADV VQSVDSVRLA
VALDAAAAAV RDRPLDVLVQ VSIDGDAARG GALPGVGDPD RGLDPVAEAV AGSAGLRLAG
LMAVAPLGWE PERAFARLAE VAERFRARHP GATVLSAGMS GDLESAIGYG ATHVRVGSAL
LGMRPTLR
//