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Database: UniProt
Entry: A0A088F218_9SPHI
LinkDB: A0A088F218_9SPHI
Original site: A0A088F218_9SPHI 
ID   A0A088F218_9SPHI        Unreviewed;       230 AA.
AC   A0A088F218;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=KO02_12880 {ECO:0000313|EMBL:AIM37485.1};
OS   Sphingobacterium sp. ML3W.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1538644 {ECO:0000313|EMBL:AIM37485.1, ECO:0000313|Proteomes:UP000028992};
RN   [1] {ECO:0000313|EMBL:AIM37485.1, ECO:0000313|Proteomes:UP000028992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML3W {ECO:0000313|EMBL:AIM37485.1};
RX   PubMed=25614576;
RA   Smith S.A., Krasucki S.P., McDowell J.V., Balke V.L.;
RT   "Complete Genome Sequence of Sphingobacterium sp. Strain ML3W, Isolated
RT   from Wings of Myotis lucifugus Infected with White Nose Syndrome.";
RL   Genome Announc. 3:0-0(2015).
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; CP009278; AIM37485.1; -; Genomic_DNA.
DR   RefSeq; WP_038698742.1; NZ_CP009278.1.
DR   AlphaFoldDB; A0A088F218; -.
DR   STRING; 1538644.KO02_12880; -.
DR   KEGG; sht:KO02_12880; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_1_3_10; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000028992; Chromosome.
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.
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:UP000028992}.
FT   DOMAIN          3..220
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         26
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   230 AA;  26274 MW;  7B6E3B3D795967F5 CRC64;
     MSIASNLEAI NLEVKALGVQ LVAVSKTKPN EDIMKAYEAG QRVFGENLVQ ELVEKYESLP
     KDIEWHLIGH LQSNKVKYIA PFVTLIHSVD SFKLLKEIDK QAAKNKRTID CLLQVDIAEE
     DTKFGFDHIE LVEMLRDEEF LALKHINIRG LMGIATNTEN EKEIKEEFYE LKSLYDGIKA
     SFYRKNENFD TLSMGMSSDY KLAIEKGSTM VRLGSTIFGK RVIKHLKNND
//
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