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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//