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Database: UniProt/TrEMBL
Entry: A0A0N9XXX6_MYCFO
LinkDB: A0A0N9XXX6_MYCFO
Original site: A0A0N9XXX6_MYCFO 
ID   A0A0N9XXX6_MYCFO        Unreviewed;       247 AA.
AC   A0A0N9XXX6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ECO:0000313|EMBL:STZ89079.1};
GN   ORFNames=A5751_21600 {ECO:0000313|EMBL:OBF78129.1}, NCTC1542_03867
GN   {ECO:0000313|EMBL:STZ89079.1}, XA26_52180
GN   {ECO:0000313|EMBL:ALI29012.1};
OS   Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1766 {ECO:0000313|EMBL:ALI29012.1, ECO:0000313|Proteomes:UP000057134};
RN   [1] {ECO:0000313|EMBL:ALI29012.1, ECO:0000313|Proteomes:UP000057134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:ALI29012.1,
RC   ECO:0000313|Proteomes:UP000057134};
RX   PubMed=26507234; DOI=10.1128/mBio.01520-15;
RA   Costa K.C., Bergkessel M., Saunders S., Korlach J., Newman D.K.;
RT   "Enzymatic Degradation of Phenazines Can Generate Energy and Protect
RT   Sensitive Organisms from Toxicity.";
RL   MBio 6:e01520-e01515(2015).
RN   [2] {ECO:0000313|Proteomes:UP000093878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852002-51695_SCH5383401 {ECO:0000313|Proteomes:UP000093878};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA   Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OBF78129.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852002-51695_SCH5383401 {ECO:0000313|EMBL:OBF78129.1};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:STZ89079.1, ECO:0000313|Proteomes:UP000255389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC1542 {ECO:0000313|EMBL:STZ89079.1,
RC   ECO:0000313|Proteomes:UP000255389};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_01039,
CC         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; CP011269; ALI29012.1; -; Genomic_DNA.
DR   EMBL; LZIH01000188; OBF78129.1; -; Genomic_DNA.
DR   EMBL; UGQY01000003; STZ89079.1; -; Genomic_DNA.
DR   RefSeq; WP_054603398.1; NZ_VHPZ01000055.1.
DR   AlphaFoldDB; A0A0N9XXX6; -.
DR   STRING; 1766.XA26_52180; -.
DR   GeneID; 83878062; -.
DR   KEGG; mft:XA26_52180; -.
DR   PATRIC; fig|1766.6.peg.5192; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000057134; Chromosome.
DR   Proteomes; UP000093878; Unassembled WGS sequence.
DR   Proteomes; UP000255389; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057134}.
FT   REGION          116..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        9
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        87
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         8..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         21..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         87..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         114..115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         181..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            180
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   247 AA;  27349 MW;  0A13A342F327F19E CRC64;
     MPTLILLRHG ESDWNQKNLF TGWVDVDLTD KGRAEAIRGG KLLVEQDVLP DVVYTSLLRR
     AITTANLALD AADRHWIPVH RDWRLNERHY GALQGLDKAA TKEKFGEEQF MAWRRSYDTP
     PPPIEKGSEF SQDSDPRYAD IGGGPLTECL KDVVERFVPY YENTIVPDLR AGKTVLIAAH
     GNSLRALVKY LDQMSDEEVV GLNIPTGIPL RYELDENLKP LVAGGEYLDP EAAAAGAAAV
     AAQGAKK
//
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