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Database: UniProt
Entry: A0A286TY78_9BACT
LinkDB: A0A286TY78_9BACT
Original site: A0A286TY78_9BACT 
ID   A0A286TY78_9BACT        Unreviewed;       243 AA.
AC   A0A286TY78;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
DE            Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
GN   ORFNames=SCALIN_C14_0114 {ECO:0000313|EMBL:GAX60848.1};
OS   Candidatus Scalindua japonica.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Scalinduaceae; Scalindua.
OX   NCBI_TaxID=1284222 {ECO:0000313|EMBL:GAX60848.1, ECO:0000313|Proteomes:UP000218542};
RN   [1] {ECO:0000313|Proteomes:UP000218542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=husup-a2 {ECO:0000313|Proteomes:UP000218542};
RA   Oshiki M., Mizuto K., Kimura Z., Kindaichi T., Satoh H., Okabe S.;
RT   "Genetic Diversity of Marine Anaerobic Ammonium-Oxidizing Bacteria as
RT   Revealed by Genomic and Proteomic Analyses of 'Candidatus Scalindua
RT   japonica'.";
RL   Environ. Microbiol. Rep. 0:0-0(2017).
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC       involved in PLP homeostasis. {ECO:0000256|HAMAP-Rule:MF_02087}.
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_02087,
CC       ECO:0000256|RuleBase:RU004514}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAX60848.1}.
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DR   EMBL; BAOS01000014; GAX60848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286TY78; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000218542; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00635; PLPDE_III_YBL036c_like; 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   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218542}.
FT   DOMAIN          6..228
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   243 AA;  27346 MW;  F6D7E2494A9F15A9 CRC64;
     MSIKENLEKV KQKIAYAAAK VGKKPEEITL VMATKTVDAE RIREAVKNGG HVIAENKIQE
     ALKKYDVLKD EDAAWHFIGH LQTNKVKDVL KFADMIHSVD RMGLVEKLDK RLMSEGRSMD
     VLIQVNTSYE ESKYGVAPEE AISLVREASQ YDTLNIRGLM TIGLFTDDEV KIRKCFKLLK
     GIHDSVIKEG IKGVEMEYLS MGMSGDYHIA IEEGANMVRV GTAIFGARDT PDAYYWPSEK
     TDK
//
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