ID A0A0D0CHR4_9AGAR Unreviewed; 301 AA.
AC A0A0D0CHR4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
DE Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
GN ORFNames=GYMLUDRAFT_48803 {ECO:0000313|EMBL:KIK54443.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK54443.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK54443.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK54443.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be
CC involved in intracellular homeostatic regulation of pyridoxal 5'-
CC phosphate (PLP), the active form of vitamin B6. {ECO:0000256|HAMAP-
CC Rule:MF_03225}.
CC -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_03225,
CC ECO:0000256|RuleBase:RU004514}.
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DR EMBL; KN834816; KIK54443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0CHR4; -.
DR HOGENOM; CLU_059988_2_0_1; -.
DR OrthoDB; 21261at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR CDD; cd06822; PLPDE_III_YBL036c_euk; 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 SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS01211; UPF0001; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03225};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593}.
FT DOMAIN 22..162
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT REGION 149..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03225"
SQ SEQUENCE 301 AA; 32471 MW; 38F840AB5DC69AEB CRC64;
MSLEPSAQQA SSERTEELCE SLAEIRARVT AAAGSAPASE PPQKLVAVSK YKPSSDISVC
FNEGQRDFGE NYVQELVDKA NELPLEIRWH FIGTLQSNKA KLLASIPNLH TVQTLSSEKV
ANALNKALPP SRTTPLNILI QINTSGEDAK SGLPPLTASS ICTSPSTSPS SNSPPSELQK
LAKHIITSCP NLRLQGLMTI GSLDQSLSAK ETDQNADFER LKETRDILQK WLQSELGESS
STKGEETEGV QRWGDEGTGK LLLSMGMSSD FEAALKAGSD IVRVGTGIFG SRKTKDEMKR
L
//
