ID   A0A178E0X8_9PLEO        Unreviewed;       710 AA.
AC   A0A178E0X8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=IQ07DRAFT_622048 {ECO:0000313|EMBL:OAL49626.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL49626.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL49626.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL49626.1,
RC   ECO:0000313|Proteomes:UP000077535};
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   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_03225}.
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DR   EMBL; KV441646; OAL49626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E0X8; -.
DR   STRING; 765867.A0A178E0X8; -.
DR   InParanoid; A0A178E0X8; -.
DR   OrthoDB; 1446241at2759; -.
DR   Proteomes; UP000077535; 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   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   HAMAP; MF_02087; PLP_homeostasis; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; SSF53474; alpha/beta-Hydrolases; 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:UP000077535}.
FT   DOMAIN          469..703
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   REGION          209..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         493
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03225"
SQ   SEQUENCE   710 AA;  78909 MW;  E5B4D7EA46989338 CRC64;
     MGVLEFICDR RFHNIFILPP DPEAGRTKPY RVSYSDYGDP NSNAVVLLCG ALMGTRLSYS
     PLDTLAKAHN VRIIHADRPG IGGTDPVDVD QRVQIWLDVV PQLLAHLNIR HVSLASHSAG
     TIYLINTLLT YPHLLHPSNP YVCFFAPWVH PAHSKVMHMQ AAELLPAPMI GKFSSVARFV
     NEKVMPLAGL SGSFVEGLKG SFMRSNGQPA PVALAPTTNR SRGNSIGSRD GSYSLPLDDE
     ETVQELRKLI MQYLFAESID GVSADTQLVL KRPRSIPWSS QSIPWNDYNE VLPLVLRMIG
     ENRNHQDGGA ERKWVVDAFH AETDDLVGDK GREWFDDCWN VANVPAPSEH DSQSPSTSNF
     EFRTQIVKDS DHNYLMDPAF GASDLWLQRV REAFPSEVDS LSLKQVGDEK KTKFRLFLNK
     LSHMTHGVTI FKSLTPSILS SNMLIVRTRS GRDYMQINPQ RAKQLAENLA SISSRISAAS
     TGSKQVRLIA VSKLKPATDI LSLHQHPGPL QTHFGENYVQ ELLEKSKLLP RSIRWHMIGG
     LQSNKCKQLA EQIPNLWCVS SVDSEKKANE LEKGRKALLE KDSEAQKLRI MVQVNTSGEE
     SKSGVEPSDT LALCQHIANK CPHLQLTGLM TIGAIARSKE TTAENENEDF ECLRDTRDQV
     AKGLAWEKEQ LELSMGMSSD FEGAIAQGSD EVRVGSDIFG ERPPKKDAVV
//