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Database: UniProt
Entry: A0A090II54_9GAMM
LinkDB: A0A090II54_9GAMM
Original site: A0A090II54_9GAMM 
ID   A0A090II54_9GAMM        Unreviewed;       231 AA.
AC   A0A090II54;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=MVIS_4097 {ECO:0000313|EMBL:CED61976.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED61976.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LN554852; CED61976.1; -; Genomic_DNA.
DR   RefSeq; WP_045112035.1; NZ_FRDR01000088.1.
DR   AlphaFoldDB; A0A090II54; -.
DR   STRING; 80854.MVIS_4097; -.
DR   KEGG; mvs:MVIS_4097; -.
DR   PATRIC; fig|80854.5.peg.4347; -.
DR   HOGENOM; CLU_059988_0_1_6; -.
DR   Proteomes; UP000032438; Chromosome complete sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06824; PLPDE_III_Yggs_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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032438}.
FT   DOMAIN          30..230
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   COILED          167..194
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   231 AA;  26000 MW;  0AA45E5A3FDCFB58 CRC64;
     MNSISTRLQQ VLTQIENTAS TSCKKRCEIN LLAVSKTKPV EQVMAVYALG QRKFGENYLQ
     EAVEKITHLQ HDGDYDDIEW HFIGPIQSNK TRPIAEHFDW VQSIDRLKVA QRLNDQRPAE
     MAKLNVCIQI NISAEDSKSG ADLQQARLLA EQVANLPNLV LRGIMAIPEK TDDLEKLKSQ
     FNQLESLYLS LQHQYNQIDT LSMGMTNDME LAIAQGSNMV RVGTAIFGAR G
//
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