ID U2Q904_LEPWF Unreviewed; 208 AA.
AC U2Q904;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) {ECO:0000256|ARBA:ARBA00012028};
DE EC=5.4.2.11 {ECO:0000256|ARBA:ARBA00012028};
GN ORFNames=HMPREF9015_00819 {ECO:0000313|EMBL:ERK52554.1};
OS Leptotrichia wadei (strain F0279).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=888055 {ECO:0000313|EMBL:ERK52554.1, ECO:0000313|Proteomes:UP000016626};
RN [1] {ECO:0000313|EMBL:ERK52554.1, ECO:0000313|Proteomes:UP000016626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0279 {ECO:0000313|EMBL:ERK52554.1,
RC ECO:0000313|Proteomes:UP000016626};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717}.
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:ERK52554.1}.
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DR EMBL; AWVM01000041; ERK52554.1; -; Genomic_DNA.
DR RefSeq; WP_021746419.1; NZ_KI271411.1.
DR AlphaFoldDB; U2Q904; -.
DR PATRIC; fig|888055.3.peg.785; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_0_0; -.
DR Proteomes; UP000016626; Unassembled WGS sequence.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF24; PHOSPHOGLYCERATE MUTASE (2,3-DIPHOSPHOGLYCERATE-DEPENDENT); 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT ACT_SITE 12
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 95
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 11..18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 208 AA; 24411 MW; A8FE2E2B38EF8830 CRC64;
MDNELKLYIV RHGQTEWNVL EKFQGQLNSP LTLEGIEKVK ETAEKLKNIK FKAGYTSQMG
RTFATAKIIL QNNNYEQEKT SDQKLKLKKL PELNEIHFGE WQGMTFKETF LKFPKEAHNY
FYDVKNYNAK NIKGEELKDG LERFLKGLKK IREEQKSGNI LIVTHGTVLE LFFNYIQNKE
ADDLDERKLI GNGQYKIFTF KNGKYVTL
//