APGM_PYRHO
ID APGM_PYRHO Reviewed; 412 AA.
AC O57742;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
DE Short=BPG-independent PGAM;
DE Short=Phosphoglyceromutase;
DE Short=aPGAM;
DE EC=5.4.2.12;
GN Name=apgM; OrderedLocusNames=PH0037;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000250}.
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;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000305}.
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DR EMBL; BA000001; BAA29105.1; -; Genomic_DNA.
DR PIR; B71222; B71222.
DR PDB; 2ZKT; X-ray; 2.40 A; A/B=1-412.
DR PDBsum; 2ZKT; -.
DR AlphaFoldDB; O57742; -.
DR SMR; O57742; -.
DR STRING; 70601.3256422; -.
DR EnsemblBacteria; BAA29105; BAA29105; BAA29105.
DR KEGG; pho:PH0037; -.
DR eggNOG; arCOG01696; Archaea.
DR OMA; IAFRCNF; -.
DR UniPathway; UPA00109; UER00186.
DR EvolutionaryTrace; O57742; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..412
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000138145"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 313..331
FT /evidence="ECO:0007829|PDB:2ZKT"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2ZKT"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:2ZKT"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:2ZKT"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:2ZKT"
SQ SEQUENCE 412 AA; 45420 MW; E10944A6762DF6D4 CRC64;
MVLKRKGLLI ILDGLGDRPI KELNGLTPLE YANTPNMDKL AEIGILGQQD PIKPGQPAGS
DTAHLSIFGY DPYETYRGRG FFEALGVGLD LSKDDLAFRV NFATLENGII TDRRAGRIST
EEAHELARAI QEEVDIGVDF IFKGATGHRA VLVLKGMSRG YKVGDNDPHE AGKPPLKFSY
EDEDSKKVAE ILEEFVKKAQ EVLEKHPINE RRRKEGKPIA NYLLIRGAGT YPNIPMKFTE
QWKVKAAGVI AVALVKGVAR AVGFDVYTPE GATGEYNTNE MAKAKKAVEL LKDYDFVFLH
FKPTDAAGHD NKPKLKAELI ERADRMIGYI LDHVDLEEVV IAITGDHSTP CEVMNHSGDP
VPLLIAGGGV RTDDTKRFGE REAMKGGLGR IRGHDIVPIM MDLMNRSEKF GA
