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Database: UniProt
Entry: I1IHW1_BRADI
LinkDB: I1IHW1_BRADI
Original site: I1IHW1_BRADI 
ID   I1IHW1_BRADI            Unreviewed;       493 AA.
AC   I1IHW1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Metalloenzyme domain-containing protein {ECO:0000259|Pfam:PF01676};
GN   Name=100846025 {ECO:0000313|EnsemblPlants:KQJ86483};
GN   ORFNames=BRADI_4g05830v3 {ECO:0000313|EMBL:KQJ86483.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQJ86483};
RN   [1] {ECO:0000313|EMBL:KQJ86483.1, ECO:0000313|EnsemblPlants:KQJ86483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ86483.1,
RC   ECO:0000313|EnsemblPlants:KQJ86483};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQJ86483.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ86483.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQJ86483}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ86483};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.12; Evidence={ECO:0000256|ARBA:ARBA00000370};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
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DR   EMBL; CM000883; KQJ86483.1; -; Genomic_DNA.
DR   RefSeq; XP_003575788.1; XM_003575740.3.
DR   AlphaFoldDB; I1IHW1; -.
DR   STRING; 15368.I1IHW1; -.
DR   EnsemblPlants; KQJ86483; KQJ86483; BRADI_4g05830v3.
DR   GeneID; 100846025; -.
DR   Gramene; KQJ86483; KQJ86483; BRADI_4g05830v3.
DR   KEGG; bdi:100846025; -.
DR   eggNOG; ENOG502QR26; Eukaryota.
DR   HOGENOM; CLU_034906_0_0_1; -.
DR   InParanoid; I1IHW1; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 313745at2759; -.
DR   Proteomes; UP000008810; Chromosome 4.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd16011; iPGM_like; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR   InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR   PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01676; Metalloenzyme; 2.
DR   Pfam; PF10143; PhosphMutase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT   DOMAIN          9..300
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          322..404
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   493 AA;  52671 MW;  3DDABAFCB8C3107C CRC64;
     MSAAAGASRV AFVLVDGIGD VTIPSIGGRT PLEAAAAPRL DAVASAGVAG LMDPVEPGLA
     CGSDTAHLSL LGYDPRVYYR GRGAFESMGA GLAMAPGDIA FKSNFATLDE STGVIVSRRA
     DRHFEEEGPI LCAALDGMKL PSFPEYEVRV RYATEHRCGV VVKGPRLSGN ISGTDPLKDN
     RLHLKAEPLD DSEEAKNTAA VVNELSKEIT RILVSQPINA KRAAEGKNIA NVVLLRGCGI
     RIEVPAFETK HGLAPCMVAP TKIIAGLGLS LGIDILEAPG ATGDYRTLLT SKAKAIAKAL
     SAPLETPPRV FVPGEDEYKA GRENGYDFGF LHIKAIDDAG HDKAVKLKVR GLEAVDQAIG
     QLARLLWEAE KSGHYQYFIC VTGDHSTPVE YGDHSFEPVP FAICRLRDFV GAFGEDNVMS
     TPLDDFPLPS VKSGEDLTDN TELAERKHDH CKAFSGDTVY EYTEIAAARG CLGRFPGSEM
     MGIIKKFMKA KND
//
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