ID A3U8X6_CROAH Unreviewed; 219 AA.
AC A3U8X6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=CA2559_09518 {ECO:0000313|EMBL:EAP86262.1};
OS Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceibacter.
OX NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP86262.1, ECO:0000313|Proteomes:UP000002297};
RN [1] {ECO:0000313|EMBL:EAP86262.1, ECO:0000313|Proteomes:UP000002297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090
RC {ECO:0000313|Proteomes:UP000002297};
RX PubMed=20639333; DOI=10.1128/JB.00733-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "The complete genome sequence of Croceibacter atlanticus HTCC2559T.";
RL J. Bacteriol. 192:4796-4797(2010).
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 ---------------------------------------------------------------------------
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; CP002046; EAP86262.1; -; Genomic_DNA.
DR RefSeq; WP_013187647.1; NC_014230.1.
DR AlphaFoldDB; A3U8X6; -.
DR STRING; 216432.CA2559_09518; -.
DR KEGG; cat:CA2559_09518; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_1_3_10; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000002297; 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:UP000002297}.
FT DOMAIN 3..216
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 25
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 219 AA; 25284 MW; 9650053E2805C64A CRC64;
MNISEQIKYY KSQLPEDVVL VAVSKTKPEE DLLEAYNAGQ RVFGENKIQE MTEKWENLPK
DIEWHMIGHV QSNKVKYMAE YVNLVHGIDR LKLIKELNKQ AQKHDRTINC LLQIKIAEED
TKFGMDINDA EAILNKDFKK TYPNVNVVGF MGMATFTNDE EQVQREFKTL KSHFDRLSKD
HNSLKILSMG MSGDYKLAIT EGSTMVRIGS AIFGERNYN
//
