ID   C7NK56_KYTSD            Unreviewed;       251 AA.
AC   C7NK56;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE            Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN   Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN   OrderedLocusNames=Ksed_03670 {ECO:0000313|EMBL:ACV05443.1};
OS   Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS   (Micrococcus sedentarius).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC   Kytococcus.
OX   NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV05443.1, ECO:0000313|Proteomes:UP000006666};
RN   [1] {ECO:0000313|EMBL:ACV05443.1, ECO:0000313|Proteomes:UP000006666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC   {ECO:0000313|Proteomes:UP000006666};
RX   PubMed=21304632; DOI=10.4056/sigs.761;
RA   Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA   Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL   Stand. Genomic Sci. 1:12-20(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|RuleBase:RU004512}.
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:0000256|ARBA:ARBA00000380,
CC         ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|RuleBase:RU004512}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC       ECO:0000256|HAMAP-Rule:MF_01039}.
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DR   EMBL; CP001686; ACV05443.1; -; Genomic_DNA.
DR   RefSeq; WP_012801861.1; NC_013169.1.
DR   AlphaFoldDB; C7NK56; -.
DR   STRING; 478801.Ksed_03670; -.
DR   KEGG; kse:Ksed_03670; -.
DR   eggNOG; COG0588; Bacteria.
DR   HOGENOM; CLU_033323_1_1_11; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000006666; 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; Phosphoglycerate mutase-like; 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   NCBIfam; TIGR01258; pgm_1; 1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01039};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01039}.
FT   REGION          118..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        13
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        91
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         12..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         25..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         91..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         118..119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            185
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   251 AA;  27891 MW;  BB6573E43958BDC9 CRC64;
     MTNAAHTLVL LRHGQSLWNE KNLFTGWVDV DLTEKGRAEA RRGGELLVAE GYLPDVLHTS
     RLRRAITTAN LALDAADRHW IDVKRSWRLN ERHYGALQGK DKAQVKDKYG EEQFMAWRRG
     YDTPPPPIEA DDEYSQAGDP RYADLGAEVP ATECLKDVVE RLRPYWAEEI VPDLQAGRTV
     LVTAHGNSLR ALVKELDGIS DADIAELNIP TGIPLVYELD GNFRPLTPGG RYLDPEAAAG
     AIQEVANQGS K
//