GPMA1_LATSS
ID GPMA1_LATSS Reviewed; 235 AA.
AC Q38ZH8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=BPG-dependent PGAM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=PGAM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=dPGM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN Name=gpmA1 {ECO:0000255|HAMAP-Rule:MF_01039}; OrderedLocusNames=LCA_0100;
OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS subsp. sakei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=314315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23K;
RX PubMed=16273110; DOI=10.1038/nbt1160;
RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA Zagorec M.;
RT "The complete genome sequence of the meat-borne lactic acid bacterium
RT Lactobacillus sakei 23K.";
RL Nat. Biotechnol. 23:1527-1533(2005).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01039};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01039}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR EMBL; CR936503; CAI54399.1; -; Genomic_DNA.
DR RefSeq; WP_011373813.1; NC_007576.1.
DR AlphaFoldDB; Q38ZH8; -.
DR SMR; Q38ZH8; -.
DR STRING; 314315.LCA_0100; -.
DR EnsemblBacteria; CAI54399; CAI54399; LCA_0100.
DR KEGG; lsa:LCA_0100; -.
DR eggNOG; COG0588; Bacteria.
DR HOGENOM; CLU_033323_1_1_9; -.
DR OMA; ITESHPY; -.
DR OrthoDB; 1122642at2; -.
DR BioCyc; LSAK314315:LCA_RS00470-MON; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002707; Chromosome.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 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; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..235
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase 1"
FT /id="PRO_0000229124"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 177
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 235 AA; 26436 MW; 307C4318329F15C2 CRC64;
MANLVIVRHG ESVANQLKTY TGWSDVALTA KGRQQAHQVG RQIKDAGFQF SHVHTSLLKR
AILTSYIVLE ELDQLALPMT KSWRLNERHY GALRGLNKDT TRTIFGVHQV ARWRRSYTAL
PPLLIRSSTA RRYRLVPRKS RPRGESLAQA TQRLLPYWQD QVVPGLLAGQ DQLIVAHGST
LRALIKVIEQ ISDQAIDGVE VANGEALYYQ FGTDLTVLKK GRLALGSETD EEKEN
