ID C9KPZ2_9FIRM Unreviewed; 230 AA.
AC C9KPZ2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=MITSMUL_05300 {ECO:0000313|EMBL:EEX68297.1};
OS Mitsuokella multacida DSM 20544.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX68297.1, ECO:0000313|Proteomes:UP000003671};
RN [1] {ECO:0000313|EMBL:EEX68297.1, ECO:0000313|Proteomes:UP000003671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX68297.1,
RC ECO:0000313|Proteomes:UP000003671};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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}.
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:EEX68297.1}.
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DR EMBL; ABWK02000020; EEX68297.1; -; Genomic_DNA.
DR RefSeq; WP_005842477.1; NZ_GG697142.2.
DR AlphaFoldDB; C9KPZ2; -.
DR STRING; 500635.MITSMUL_05300; -.
DR GeneID; 78516688; -.
DR PATRIC; fig|500635.8.peg.1933; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_1_0_9; -.
DR Proteomes; UP000003671; 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}.
FT DOMAIN 25..227
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; 25961 MW; F413B1D5866E0FDF CRC64;
MIAENLHQVE QHIKEAMARR TRVPKDAPVK LVAVTKNHDV EAMREAIDAG ATDIGENRIQ
EAKSKFDILD RDVTWHLIGH LQTNKAKQAV KYFSLIHSVD SEHLARALDK EAGKIGKCQD
VLVQVNLAKE DSKSGIYKED LRPLLDLVDA LPNLRLRGLM CIAPNYADVE ACRPLFHEMY
EIFQQVKEIP FKTANISYLS MGMTHDYQIA VEEGANIVRV GTAIFGPRQY
//
