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Database: UniProt
Entry: E1JDW6_ECOLX
LinkDB: E1JDW6_ECOLX
Original site: E1JDW6_ECOLX 
ID   E1JDW6_ECOLX            Unreviewed;       220 AA.
AC   E1JDW6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Pyridoxal phosphate enzyme, YggS family {ECO:0000313|EMBL:EFK65938.1};
DE   Flags: Fragment;
GN   ORFNames=HMPREF9347_05168 {ECO:0000313|EMBL:EFK65938.1};
OS   Escherichia coli MS 124-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK65938.1, ECO:0000313|Proteomes:UP000003390};
RN   [1] {ECO:0000313|EMBL:EFK65938.1, ECO:0000313|Proteomes:UP000003390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK65938.1,
RC   ECO:0000313|Proteomes:UP000003390};
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., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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|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:EFK65938.1}.
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DR   EMBL; ADWT01000074; EFK65938.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1JDW6; -.
DR   Proteomes; UP000003390; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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|PIRSR:PIRSR004848-1}.
FT   DOMAIN          27..215
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         22
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004848-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFK65938.1"
SQ   SEQUENCE   220 AA;  24358 MW;  AB09CDF3DAEEC58D CRC64;
     SAACNALRPF SRRNYAALQS VKQKPASAIA EAIDAGQRQF GENYVQEGVD KIRHFQELGV
     TGLEWHFIGP LQSNKSRLVA EHFDWCHTID RLRIATRLND QRPAELPPLN VLIQINISDE
     NSKSGIQLAE LDELAAAVAE LPRLRLRGLM AIPAPESEYV RQFEVARQMA VAFAGLKTRY
     PHIDTLSLGM SDDMEAAIAA GSTMVRIGTA IFGARDYSKK
//
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