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Database: UniProt
Entry: J6JAY1_9RHOB
LinkDB: J6JAY1_9RHOB
Original site: J6JAY1_9RHOB 
ID   J6JAY1_9RHOB            Unreviewed;       247 AA.
AC   J6JAY1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=A33M_1786 {ECO:0000313|EMBL:EJW12635.1};
OS   Rhodovulum sp. PH10.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW12635.1, ECO:0000313|Proteomes:UP000002930};
RN   [1] {ECO:0000313|EMBL:EJW12635.1, ECO:0000313|Proteomes:UP000002930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH10 {ECO:0000313|EMBL:EJW12635.1,
RC   ECO:0000313|Proteomes:UP000002930};
RX   PubMed=23105089; DOI=10.1128/JB.01695-12;
RA   Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT   "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT   Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT   India.";
RL   J. Bacteriol. 194:6363-6363(2012).
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:EJW12635.1}.
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DR   EMBL; AKZI01000025; EJW12635.1; -; Genomic_DNA.
DR   AlphaFoldDB; J6JAY1; -.
DR   STRING; 1187851.A33M_1786; -.
DR   PATRIC; fig|1187851.3.peg.1057; -.
DR   eggNOG; COG0325; Bacteria.
DR   Proteomes; UP000002930; 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.
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:UP000002930}.
FT   DOMAIN          28..241
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   247 AA;  26007 MW;  EEFC645375C5099A CRC64;
     MSFSAMPDSP KPSSSTAPTD VDGPAGRLAA VRREIAEACR EAGRDPASVT LVAVSKTFEA
     AAIEPVIGAG QRIFGENRVQ EAKAKWGPLA ARHPGVALHF IGPLQSNKAR EAVELFDAIH
     SVDRPSLCVA LAKEVERQGR RPLLFVEINT GAEPQKAGIL PEEADAFLEA CRTGYGLSIG
     GLMCIPPFDE PPAPHFALTA KIAARNGLEL LSMGMSDDFA TAIRFGATHV RVGTAIFGSR
     PKATAGQ
//
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