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Database: UniProt
Entry: C6VWA2_DYAFD
LinkDB: C6VWA2_DYAFD
Original site: C6VWA2_DYAFD 
ID   C6VWA2_DYAFD            Unreviewed;       220 AA.
AC   C6VWA2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 70.
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=Dfer_2011 {ECO:0000313|EMBL:ACT93234.1};
OS   Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS   52180 / NS114).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT93234.1, ECO:0000313|Proteomes:UP000002011};
RN   [1] {ECO:0000313|EMBL:ACT93234.1, ECO:0000313|Proteomes:UP000002011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC   {ECO:0000313|Proteomes:UP000002011};
RX   PubMed=21304649; DOI=10.4056/sigs.19262;
RA   Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA   Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL   Stand. Genomic Sci. 1:133-140(2009).
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; CP001619; ACT93234.1; -; Genomic_DNA.
DR   RefSeq; WP_015811486.1; NC_013037.1.
DR   AlphaFoldDB; C6VWA2; -.
DR   STRING; 471854.Dfer_2011; -.
DR   KEGG; dfe:Dfer_2011; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_1_3_10; -.
DR   OMA; IEWHMIG; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000002011; 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:UP000002011}.
FT   DOMAIN          3..219
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         26
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   220 AA;  24648 MW;  1F645707DB4D2C41 CRC64;
     MPSIADNLAQ IEQALRKETR LVAVTKTKPT TLLMEAYEAG ARLFGENKVQ EMVAKYEELP
     KDIEWHMIGH LQTNKVKYMA PFVSLVHSVD SFKLLKEINK EARKNDRIID CLLQIYIARE
     ETKFGLSEDE ALALITSPEL ATLANVRIAG LMGMASNTDD QEAVRSEFRG LKSTFEAFKN
     HENAQVTMRE LSMGMSGDYL IAMEEGSTLV RVGSAIFGSR
//
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