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Database: UniProt
Entry: D8S1G2_SELML
LinkDB: D8S1G2_SELML
Original site: D8S1G2_SELML 
ID   D8S1G2_SELML            Unreviewed;       244 AA.
AC   D8S1G2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
DE            Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
GN   ORFNames=SELMODRAFT_106172 {ECO:0000313|EMBL:EFJ21702.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ21702.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be
CC       involved in intracellular homeostatic regulation of pyridoxal 5'-
CC       phosphate (PLP), the active form of vitamin B6. {ECO:0000256|HAMAP-
CC       Rule:MF_03225}.
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_03225,
CC       ECO:0000256|RuleBase:RU004514}.
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DR   EMBL; GL377598; EFJ21702.1; -; Genomic_DNA.
DR   RefSeq; XP_002977093.1; XM_002977047.1.
DR   AlphaFoldDB; D8S1G2; -.
DR   STRING; 88036.D8S1G2; -.
DR   EnsemblPlants; EFJ21702; EFJ21702; SELMODRAFT_106172.
DR   GeneID; 9638971; -.
DR   Gramene; EFJ21702; EFJ21702; SELMODRAFT_106172.
DR   KEGG; smo:SELMODRAFT_106172; -.
DR   eggNOG; KOG3157; Eukaryota.
DR   HOGENOM; CLU_059988_2_1_1; -.
DR   InParanoid; D8S1G2; -.
DR   OMA; HIPFHLI; -.
DR   OrthoDB; 21261at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   CDD; cd06822; PLPDE_III_YBL036c_euk; 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_03225,
KW   ECO:0000256|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT   DOMAIN          18..238
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         43
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03225,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   244 AA;  26677 MW;  E462C4F8CEF6FB19 CRC64;
     MAARALPAAA AVQALRSVYE RVRVAAERSG RSASQVNVVA VSKTKPVSLI REVYDAGHRH
     FGENYVQEFI DKAPQLPSDI RWHFIGHLQS NKAKSLVANV PQLYMVEGID NFKVASLLDR
     AVSLLQRNPL KVLVQVNTSG EESKSGVEPS ACVELAKQIK ADCPNLEFSG LMTIGMQDYT
     STPENFKALV NCREDVCKAL EIPQSSCELS MGMSGDFEQA IEMGSTNVRI GSTIFGAREY
     PAKK
//
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