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Database: UniProt
Entry: A0A081CCR9_PSEA2
LinkDB: A0A081CCR9_PSEA2
Original site: A0A081CCR9_PSEA2 
ID   A0A081CCR9_PSEA2        Unreviewed;       955 AA.
AC   A0A081CCR9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=PAN0_005c2679 {ECO:0000313|EMBL:GAK64465.1}, PSANT_02712
GN   {ECO:0000313|EMBL:SPO45026.1};
OS   Pseudozyma antarctica (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK64465.1, ECO:0000313|Proteomes:UP000053758};
RN   [1] {ECO:0000313|Proteomes:UP000053758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA   Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA   Morita T.;
RT   "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT   JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT   Lipids.";
RL   Genome Announc. 2:e00878-e00814(2014).
RN   [2] {ECO:0000313|EMBL:GAK64465.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK64465.1};
RA   Morita T., Saika A., Koike H.;
RT   "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT   as a producer of lipase B which used in a wide range of industrial
RT   applications.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SPO45026.1, ECO:0000313|Proteomes:UP000325008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC   {ECO:0000313|EMBL:SPO45026.1};
RA   Guldener U.;
RL   Submitted (MAR-2018) 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; DF830072; GAK64465.1; -; Genomic_DNA.
DR   EMBL; OOIQ01000005; SPO45026.1; -; Genomic_DNA.
DR   RefSeq; XP_014657405.1; XM_014801919.1.
DR   AlphaFoldDB; A0A081CCR9; -.
DR   GeneID; 26303408; -.
DR   HOGENOM; CLU_308625_0_0_1; -.
DR   OrthoDB; 21261at2759; -.
DR   Proteomes; UP000053758; Unassembled WGS sequence.
DR   Proteomes; UP000325008; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR019140; MCM_complex-bd.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR011078; PyrdxlP_homeostasis.
DR   NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR   PANTHER; PTHR13489:SF0; MINI-CHROMOSOME MAINTENANCE COMPLEX-BINDING PROTEIN; 1.
DR   PANTHER; PTHR13489; UNCHARACTERIZED; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF09739; MCM_bind; 2.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS01211; UPF0001; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053758}.
FT   DOMAIN          214..473
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   REGION          492..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..882
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03225"
SQ   SEQUENCE   955 AA;  101577 MW;  5C7E8159A7661B7A CRC64;
     MVPDTDFTAA LNKPLEVVQK IYSDAQDKSP DNITKLVTAH FQQLFASSDA KSKIPTLSAA
     NIATLLPKAN ADAGSLHRLV RFRAMIQDTG LGTEVFLAKH QQGDRNITGL FGGEAILPAS
     ESSVDTEHAE PDHQNLAERA VMYAVSVPGQ TEWAAQAHRE AAAEASSDSS VDELTSATAA
     VALEEPQSPQ KVEEVRQRIR RAAEKGKAIG SSGKVPRLVA ISKLHPPSAI LAAHKKAGQL
     HFGENYVQEM VDKAKVLPRE IRWHFVGGLQ SNKGKLLASI PNLYLLETLD SIKAANVLQK
     ALSSPDAAKR DEPLRVYLQV NTSGEDAKSG LPPVLSTDPE QAKESELLKL AVHVITTCPN
     LRLRGVMTIG AAANSSSADA DQPKSVDEIV SANPDFERLI HTRKNLVELL RKDPDVAKAD
     QAHVKEAYAD LLEGSEANGG LELSMGMSAD MDVATMAGSD NVRVGTDCFG RRPGTREEAM
     NGMKRELEVG PEAAAEELKG SSAPSQGGAA SSSSSGADKF TLPRAYLAKS PLPEAPHVGG
     LVKLYDLEAA EKFKTTELVE VIGILDKASL PQAEWQETGS GAASGAEPAE VPCIHAVCAF
     AVELDSVRAQ ESTGGSSSGN ALAQAADRDA LITFLSGGLA GDKLAAELVL LATIARIHVR
     RANLCLGALT LNVSNFGAAG KTASSAEQTQ LSRRLNMLLP AVVDVSMELA SLNDDRKPLY
     ARSAGEGTGL EAGRLQLVNG TTIVVNEGTM GEGQLKESGI RNIRALSSVL ESHKLPYAFP
     YSEFEFDTDL NAIVLSQGKS FLPFDIHCPL SPEAGSEDLY SSSVPKDEAE QLAGWRSALL
     EARSLATAKA FEIPDSVSEH IQHEFVAERR KEQQESKDAH GGVASKEGAL GQEDLLRRMS
     LVRLLAISHA EKTLTIERWN SAVELDKQLM QRVAAAQPQS QQNPASGSAG AGVSR
//
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