ID Q72Q38_LEPIC Unreviewed; 222 AA.
AC Q72Q38;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=LIC_12276 {ECO:0000313|EMBL:AAS70847.1};
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS70847.1, ECO:0000313|Proteomes:UP000007037};
RN [1] {ECO:0000313|EMBL:AAS70847.1, ECO:0000313|Proteomes:UP000007037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS70847.1,
RC ECO:0000313|Proteomes:UP000007037};
RX PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., Ho P.L.,
RA Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F., Leite L.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H., Harakava R., Jeronimo S.M., Junqueira-De-Azevedo I.L.,
RA Kimura E.T., Kuramae E.E., Lemos E.G., Lemos M.V., Marino C.L., Nunes L.R.,
RA De Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J.,
RA Sommer P., Tsai S.M., Simpson A.J., Ferro J.A., Camargo L.E.,
RA Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS70847.1; -; Genomic_DNA.
DR RefSeq; WP_000538451.1; NC_005823.1.
DR AlphaFoldDB; Q72Q38; -.
DR GeneID; 61142161; -.
DR KEGG; lic:LIC_12276; -.
DR HOGENOM; CLU_059988_1_3_12; -.
DR Proteomes; UP000007037; Chromosome I.
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 8..221
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 30
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 222 AA; 25161 MW; AE815ACC4971C362 CRC64;
MGVLESYQKI YEELQQLRSE NPPTLIAVSK FQPIEKIKEA IGCGVVHFGE NRIQEGIEKF
SQWLKDKNTS LVLHHIGPVQ SGTLRKLFLG YSYAHGVGSV GIVNELLTRA LREEKKILYF
LQANLTGENT KHGFERKELI EILKQKEKLS NTYCKLEGLM VMGPSDGDLT KTREVFRELS
KFKKDYIPEA KLSMGMSGDY KIAIEEGSDF VRIGSAIFGE RN
//
