ID M5J4S3_9LACO Unreviewed; 223 AA.
AC M5J4S3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:EKW99443.1};
GN ORFNames=D271_01989 {ECO:0000313|EMBL:EKW99443.1};
OS Ligilactobacillus saerimneri 30a.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99443.1, ECO:0000313|Proteomes:UP000011912};
RN [1] {ECO:0000313|EMBL:EKW99443.1, ECO:0000313|Proteomes:UP000011912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30a {ECO:0000313|EMBL:EKW99443.1,
RC ECO:0000313|Proteomes:UP000011912};
RX PubMed=23405290;
RA Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA Lolkema J.S., Lucas P.M.;
RT "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT Biogenic Amines.";
RL Genome Announc. 1:E00097-E00012(2013).
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:EKW99443.1}.
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DR EMBL; ANAG01000006; EKW99443.1; -; Genomic_DNA.
DR RefSeq; WP_009552041.1; NZ_ANAG01000006.1.
DR AlphaFoldDB; M5J4S3; -.
DR STRING; 1227363.D271_01989; -.
DR GeneID; 80986296; -.
DR PATRIC; fig|1227363.6.peg.389; -.
DR Proteomes; UP000011912; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF9; PHOSPHOGLYCERATE MUTASE 2 PARALOG; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000011912}.
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 9..16
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 223 AA; 25832 MW; 62FB8793A8D03ED2 CRC64;
MAFTVYLVRH GQTESNLKGQ NQGWADTPLT LTGRRTAIET GKHLAHVAFT KAFSSDTGRA
QATARLILAQ NELTSLKQPI PLVYFREQYY GFFENVPYEQ LWAAVLHHEG YRSLDKFLNH
HDFNQTKDSF KRADPLSLAE DQYEFWSRLN RGLTYLRDHC QDGDKVLVTS HAETIGCLVQ
HYRPDLITKR EQMPENGAVT KLVFTPNNVE VVYYNHYRTD QTY
//
