APGM_THEAC
ID APGM_THEAC Reviewed; 404 AA.
AC Q9HL27;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=aPGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01402};
GN Name=apgM {ECO:0000255|HAMAP-Rule:MF_01402}; OrderedLocusNames=Ta0413;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_01402};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01402}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01402}.
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DR EMBL; AL445064; CAC11555.1; -; Genomic_DNA.
DR RefSeq; WP_010900840.1; NC_002578.1.
DR PDB; 3IDD; X-ray; 2.80 A; A/B=1-404.
DR PDB; 3KD8; X-ray; 2.60 A; A/B=2-397.
DR PDBsum; 3IDD; -.
DR PDBsum; 3KD8; -.
DR AlphaFoldDB; Q9HL27; -.
DR SMR; Q9HL27; -.
DR STRING; 273075.Ta0413; -.
DR DNASU; 1456023; -.
DR EnsemblBacteria; CAC11555; CAC11555; CAC11555.
DR GeneID; 1456023; -.
DR KEGG; tac:Ta0413; -.
DR eggNOG; arCOG01696; Archaea.
DR HOGENOM; CLU_034906_2_0_2; -.
DR OMA; IAFRCNF; -.
DR OrthoDB; 17268at2157; -.
DR BRENDA; 5.4.2.12; 6324.
DR UniPathway; UPA00109; UER00186.
DR EvolutionaryTrace; Q9HL27; -.
DR Proteomes; UP000001024; 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; 3.30.70.2130; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR HAMAP; MF_01402_A; ApgM_A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR PANTHER; PTHR31209; PTHR31209; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR TIGRFAMs; TIGR00306; apgM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..404
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000138150"
FT REGION 155..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:3KD8"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 94..110
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 182..200
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3KD8"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:3KD8"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:3KD8"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:3KD8"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3KD8"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:3KD8"
SQ SEQUENCE 404 AA; 43933 MW; 06C0306580FE8BDF CRC64;
MMKSIILIVL DGLGDRPGSD LQNRTPLQAA FRPNLNWLAS HGINGIMHPI SPGIRCGSDT
SHMSLLGYDP KVYYPGRGPF EALGLGMDIR PGDLAFRANF ATNRDGVIVD RRAGRENKGN
EELADAISLD MGEYSFRVKS GVEHRAALVV SGPDLSDMIG DSDPHREGLP PEKIRPTDPS
GDRTAEVMNA YLEEARRILS DHRVNKERVK NGRLPGNELL VRSAGKVPAI PSFTEKNRMK
GACVVGSPWL KGLCRLLRMD VFDVPGATGT VGSNYRGKIE KAVDLTSSHD FVLVNIKATD
VAGHDGNYPL KRDVIEDIDR AMEPLKSIGD HAVICVTGDH STPCSFKDHS GDPVPIVFYT
DGVMNDGVHL FDELSSASGS LRITSYNVMD ILMQLAGRSD KFGS
