ID C5WDJ8_9ENTR Unreviewed; 230 AA.
AC C5WDJ8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 Name=yggS {ECO:0000313|EMBL:BAH83404.1};
GN ORFNames=ICMP_563 {ECO:0000313|EMBL:BAH83404.1};
OS Candidatus Ishikawaella capsulata Mpkobe.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Ishikawaella.
OX NCBI_TaxID=476281 {ECO:0000313|EMBL:BAH83404.1, ECO:0000313|Proteomes:UP000061704};
RN [1] {ECO:0000313|EMBL:BAH83404.1, ECO:0000313|Proteomes:UP000061704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mpkobe {ECO:0000313|EMBL:BAH83404.1,
RC ECO:0000313|Proteomes:UP000061704};
RX PubMed=21737395;
RA Nikoh N., Hosokawa T., Ohshima K., Hattori M., Fukatsu T.;
RT "Reductive evolution of bacterial genome in insect gut environment.";
RL Genome Biol. Evol. 3:702-714(2011).
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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02087}.
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; AP010872; BAH83404.1; -; Genomic_DNA.
DR RefSeq; WP_041069747.1; NZ_AP010872.1.
DR AlphaFoldDB; C5WDJ8; -.
DR STRING; 476281.ICMP_563; -.
DR KEGG; icp:ICMP_563; -.
DR HOGENOM; CLU_059988_0_1_6; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000061704; Chromosome.
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 Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW ECO:0000256|PIRSR:PIRSR004848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061704}.
FT DOMAIN 27..228
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
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 230 AA; 26236 MW; 685C191D93908762 CRC64;
MISIKENLNE VRNQIMLHAI KYQRHPKDIK LLAVSKNKSI SEIKEAIKFG QRFFGENYVQ
EAIKKIQQLN NFLSVEWHFI GTVQSNKSRL VAENFTWCHT INSLKIAQRL NDQRPTYLPP
LNVLIQINIS GEDSKSGVDL NILPTLAKVI NNNLPYLKLR GLMTIPAREK DYKLQFSIYQ
KMSKIFHSMK LQYPDIDTLS LGMSDDMAAA IAAGSTLLRI GTAIFGSRDK
//