ID   D2C841_THEP2            Unreviewed;       401 AA.
AC   D2C841;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01402};
DE            Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01402};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01402};
DE            Short=aPGAM {ECO:0000256|HAMAP-Rule:MF_01402};
DE            EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01402};
GN   Name=apgM {ECO:0000256|HAMAP-Rule:MF_01402};
GN   OrderedLocusNames=Tnap_1040 {ECO:0000313|EMBL:ADA67127.1};
OS   Thermotoga petrophila (strain ATCC BAA-489 / DSM 13996 / JCM 10882 /
OS   RKU-10) (Thermotoga naphthophila).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=590168 {ECO:0000313|EMBL:ADA67127.1, ECO:0000313|Proteomes:UP000000940};
RN   [1] {ECO:0000313|EMBL:ADA67127.1, ECO:0000313|Proteomes:UP000000940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-489 / DSM 13996 / JCM 10882 / RKU-10
RC   {ECO:0000313|Proteomes:UP000000940};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K.E., Gogarten J.P., Noll K.M.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315, ECO:0000256|HAMAP-
CC       Rule:MF_01402}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.12; Evidence={ECO:0000256|ARBA:ARBA00000370,
CC         ECO:0000256|HAMAP-Rule:MF_01402};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC       Rule:MF_01402}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524,
CC       ECO:0000256|HAMAP-Rule:MF_01402}.
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DR   EMBL; CP001839; ADA67127.1; -; Genomic_DNA.
DR   RefSeq; WP_012896315.1; NC_013642.1.
DR   AlphaFoldDB; D2C841; -.
DR   KEGG; tnp:Tnap_1040; -.
DR   HOGENOM; CLU_034906_2_0_0; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000940; Chromosome.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16011; iPGM_like; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR   HAMAP; MF_01402_B; ApgM_B; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR023665; ApgAM_prokaryotes.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR   NCBIfam; TIGR00306; apgM; 1.
DR   PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   Pfam; PF10143; PhosphMutase; 1.
DR   PIRSF; PIRSF006392; IPGAM_arch; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01402};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01402};
KW   Pyruvate {ECO:0000313|EMBL:ADA67127.1}.
FT   DOMAIN          18..390
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   401 AA;  44335 MW;  566E258CD8BE2C22 CRC64;
     MFDKQEFVSK LVTEEKAKIV LLVMDGLGDI PVNGKTPLQA ANTPNLDNLA KESDLGQTIP
     VLPGITPGSG PGHLSLFGYD PIRYQIGRGI LEALGIGVEV GEKDVVARAN FATWDGKVVL
     DRRAGRPATE ESSKVVQLLS EKIKKIEDVE ITFYPGKEHR FVVKFTGEGL GDNVTDADPQ
     KEGHPMVWAE GLDEPSKKTA RITNELIKKI AEVLKDNPKI NFALIRGFSK YPDLPKFPQV
     YKMKAGAIAT YPMYRGLAKL VGMEIIETGQ TVADEIKTLK ERWNDYDFFY VHVKKTDSYG
     EDGKFEEKVK VIEEVDALIP EIVSLNPDVL VITGDHSTPV PLKAHSWHPV PLLIWSKYTR
     RGLSQAFNEF ECARGTLGTI HASDVMTLAL AYAGKLEKFG A
//