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Database: UniProt
Entry: A0A1J4JYN8_9EUKA
LinkDB: A0A1J4JYN8_9EUKA
Original site: A0A1J4JYN8_9EUKA 
ID   A0A1J4JYN8_9EUKA        Unreviewed;       612 AA.
AC   A0A1J4JYN8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE            EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
GN   Name=gpmI {ECO:0000313|EMBL:OHT04279.1};
GN   ORFNames=TRFO_28268 {ECO:0000313|EMBL:OHT04279.1};
OS   Tritrichomonas foetus.
OC   Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC   Tritrichomonas.
OX   NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT04279.1, ECO:0000313|Proteomes:UP000179807};
RN   [1] {ECO:0000313|Proteomes:UP000179807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA   Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA   Tasca T., Bogo M.R., de Souza W.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000256|ARBA:ARBA00008819}.
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:OHT04279.1}.
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DR   EMBL; MLAK01000799; OHT04279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4JYN8; -.
DR   VEuPathDB; TrichDB:TRFO_28268; -.
DR   OrthoDB; 212at2759; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000179807; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR011258; BPG-indep_PGM_N.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR036646; PGAM_B_sf.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF06415; iPGM_N; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179807};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..612
FT                   /note="phosphoglycerate mutase (2,3-diphosphoglycerate-
FT                   independent)"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013131327"
FT   TRANSMEM        561..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..519
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          113..298
FT                   /note="BPG-independent PGAM N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06415"
SQ   SEQUENCE   612 AA;  68935 MW;  A41CA931D98EBD30 CRC64;
     MADRYFKMHL FTILFLITQS SPKGAVLTVI DGFGESAWPE GNGIQSAKMT FLDSLRSQFP
     YQSLVAAQQP VGLVRGEPGS SAVGHQTLGL GRTTPSYFQV LERSMNRKAP EAMINNKVLR
     DAFHTTKRAH FVGLCTDEGI FSHVKFLPPM FEAAAIENVS EVYVHCILTT LTDKPSNYLN
     KVESYFPKEL GTRIKIAGVY SGETAMDKMR NWTMTQIAYD GMTNPKKAKP MSKYKAYKYL
     DSIGQIVPEF DPICIEYEKN SCNNSIMKPD DVVVYFHFRE DKSYQLAKAL IDGMKGSKNP
     KLRVLSLILF DKSLYNRSTL IIPAVKYNNT LPAVISQHGY KQLRVAEEYK RSHATIFFSG
     GIMQPIYPGE DRAVDFTSPA EKVVDLYPEM NASLITKAAI EGINKNEYKL IFINYANVDA
     TGHTGNQTAV KIAAEFVDQQ VKKIYEECIK NDYLLFITSD HGNGEELIEL NGELQLYHTV
     NNVPFIVCSN KYEIVPSQTG KVPFIGNVAP SILYALGIEI PKEMEPPIIR KSLKINEKVT
     LDMNDWQAHD SNLSISRSHQ TLLLGFILGV LTTILSIFIS RFMQIRICGI LFGVRETRKE
     RRDSWNHSNI SV
//
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