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Entry: I1LRD0_SOYBN
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ID   I1LRD0_SOYBN            Unreviewed;       502 AA.
AC   I1LRD0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=2-carboxy-D-arabinitol-1-phosphatase {ECO:0008006|Google:ProtNLM};
GN   Name=100794084 {ECO:0000313|EnsemblPlants:KRH25174};
GN   ORFNames=GLYMA_12G085900 {ECO:0000313|EMBL:KRH25174.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH25174.1};
RN   [1] {ECO:0000313|EMBL:KRH25174.1, ECO:0000313|EnsemblPlants:KRH25174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH25174};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH25174.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH25174}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH25174};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH25174.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH25174.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000256|ARBA:ARBA00038362}.
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DR   EMBL; CM000845; KRH25174.1; -; Genomic_DNA.
DR   RefSeq; XP_003539810.1; XM_003539762.3.
DR   AlphaFoldDB; I1LRD0; -.
DR   SMR; I1LRD0; -.
DR   STRING; 3847.I1LRD0; -.
DR   PaxDb; 3847-GLYMA12G09100-1; -.
DR   EnsemblPlants; KRH25174; KRH25174; GLYMA_12G085900.
DR   GeneID; 100794084; -.
DR   Gramene; KRH25174; KRH25174; GLYMA_12G085900.
DR   KEGG; gmx:100794084; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   HOGENOM; CLU_035286_0_0_1; -.
DR   InParanoid; I1LRD0; -.
DR   OMA; RFQGQID; -.
DR   OrthoDB; 1217469at2759; -.
DR   Proteomes; UP000008827; Chromosome 12.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 2.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 2.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT   ACT_SITE        67
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        141
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         66..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   502 AA;  55245 MW;  F241AEBEF4BFBF2A CRC64;
     MFLVVRACGS SSAHIQPTLT PQRSSINVVV RCSISSVQEK EEKGTELDSS VSFPLIRAAK
     RVVLVRHGQS TWNAEGRIQG SSNFSVLTKK GESQAETSRQ MLIDDHFDAC FASPLARSKR
     TAEIIWGPRH EPIIPDYDLR EIDLYSFQGL LKHEGKERFG SAFRQWQVDA ANFIIDGHYP
     VRELWERARS CWTRILAHDS RSVLVVAHNA VNQALVGTAI GLGPEYFRTL LQSNCGVSVL
     DFIPRSEGGS PHICLNRLNQ TPGSPIAGGK SGGRESSKRI ILICNGSTQG NTEDVFPFGG
     DQPLNMLGVI QSQKSAELLL DLKVNSIISS PNKACVGTAT IISQVQEAAD CLGADCVPRY
     VEMKQMGNFD VETLFKQSEM DISNFPPFQP GWLNRVDDGL RTTLWDQSGK TWQSLLDEID
     ESNTEVVVAV GHPAKHIALM GHCLNLTKEW LGSFHLDAGS VSVVDFPDGP KGKGVIRCIN
     YTAHLGRWSI PITRSTEDGE EF
//
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