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Database: UniProt
Entry: C6RAW4_9CORY
LinkDB: C6RAW4_9CORY
Original site: C6RAW4_9CORY 
ID   C6RAW4_9CORY            Unreviewed;       232 AA.
AC   C6RAW4;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=CORTU0001_1744 {ECO:0000313|EMBL:EET77215.1};
OS   Corynebacterium tuberculostearicum SK141.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=553206 {ECO:0000313|EMBL:EET77215.1, ECO:0000313|Proteomes:UP000004384};
RN   [1] {ECO:0000313|EMBL:EET77215.1, ECO:0000313|Proteomes:UP000004384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK141 {ECO:0000313|EMBL:EET77215.1,
RC   ECO:0000313|Proteomes:UP000004384};
RA   Dodson R., Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Strausberg R.L., Nelson K.E.;
RL   Submitted (JUN-2009) 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:EET77215.1}.
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DR   EMBL; ACVP01000023; EET77215.1; -; Genomic_DNA.
DR   RefSeq; WP_005328907.1; NZ_ACVP01000023.1.
DR   AlphaFoldDB; C6RAW4; -.
DR   Proteomes; UP000004384; 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.
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          11..230
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         38
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   232 AA;  24864 MW;  C353B9373745E7F6 CRC64;
     MSDRKAQLEH NLSATLAKIE RLAAQSGRKP PQLLPVTKFH PAADIALLAE LGVTDVAENR
     EQEARAKATE LPQLRFHMIG QIQTKKANHV ARWAASVHSL DSLKLAHALE RGVSLAKERG
     ERESNLPVFI QVSADGDGAR GGVSPEALDE LVRAVEEAQH LELAGLMVVP PLDADAGEVF
     RNVRGEVDRL SSELNRPLKF SAGMSADMAE AIAAGSDIVR VGTSIMGPRP VG
//
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