ID A0A178AV39_9PLEO Unreviewed; 271 AA.
AC A0A178AV39;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
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=IQ06DRAFT_293834 {ECO:0000313|EMBL:OAL00508.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL00508.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL00508.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL00508.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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 -!- 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_03225,
CC ECO:0000256|RuleBase:RU004514}.
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DR EMBL; KV441712; OAL00508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AV39; -.
DR STRING; 765868.A0A178AV39; -.
DR InParanoid; A0A178AV39; -.
DR OrthoDB; 21261at2759; -.
DR Proteomes; UP000077206; 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 PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS01211; UPF0001; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03225,
KW ECO:0000256|PIRSR:PIRSR004848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 18..255
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT REGION 249..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..222
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 257..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03225,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 271 AA; 30064 MW; EC3C90BE3310C48C CRC64;
MADDMQINPQ RAKQLTENLS SITSRIAAAN KSNRNVRLIA VSKLKPANDI LALHQAPNPL
HTHFGENYVQ ELLEKSKLLP RSIRWHMIGG LQSNKCKQLA EQIPNLWCVS SVDSVKKANE
LEKGRKALLE KDGSEGVDKL RVMIQVNTSG ESEKSGVEPA DATALCRHVL DNCPHLELLG
LMTIGAIARS QATTEENENE DFEKLRETRD KVAEELEWEK EKLELSMGMS ADFEGAIRAG
SDEVRVGSQI FGERPAKGDA VIKEKEAEEK S
//