ID I4MD39_GARVA Unreviewed; 272 AA.
AC I4MD39;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:EIK87129.1};
GN ORFNames=CGSMWGv6119V5_05671 {ECO:0000313|EMBL:EIK87129.1};
OS Gardnerella vaginalis 6119V5.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=698961 {ECO:0000313|EMBL:EIK87129.1, ECO:0000313|Proteomes:UP000033041};
RN [1] {ECO:0000313|EMBL:EIK87129.1, ECO:0000313|Proteomes:UP000033041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6119V5 {ECO:0000313|EMBL:EIK87129.1,
RC ECO:0000313|Proteomes:UP000033041};
RX PubMed=22609915; DOI=10.1128/JB.00056-12;
RA Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT Consistent with Subspeciation into Genovars.";
RL J. Bacteriol. 194:3922-3937(2012).
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:EIK87129.1}.
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DR EMBL; ADEW01000011; EIK87129.1; -; Genomic_DNA.
DR RefSeq; WP_004137485.1; NZ_ADEW01000011.1.
DR AlphaFoldDB; I4MD39; -.
DR PATRIC; fig|698961.3.peg.1128; -.
DR eggNOG; COG0406; Bacteria.
DR OrthoDB; 4697614at2; -.
DR Proteomes; UP000033041; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF68; GLUCOSYL-3-PHOSPHOGLYCERATE PHOSPHATASE; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
FT ACT_SITE 32
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 131
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 31..38
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 272 AA; 30033 MW; 28244BAEC48CB3B7 CRC64;
MVDFVENVAS NVNNSINSTH EGIARSVMLI RHGQTPYNAQ FRLQGMIDIA LDESGMDQVT
RSGKALRVLF GASDLEDPKD PNSAEHVRIT PEEADASFVA IVSPLIRAQQ TAHAFADKLG
LHVHVENGVR ERFFGEWEGL NRKQISEKWP EDFNAWVKGE GGELRHGAET KQEVGERAAA
TVEQWTRKTG SDRDLLVFSH GSCLSQTVHK LLGLDKVDPS YKTIGGMGNG RWARLIPSLN
ADGSIHWRLD AYDQGPAADP TSQRLIRIWG AA
//
