ID A0A0U5AGK0_9BACT Unreviewed; 408 AA.
AC A0A0U5AGK0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=THC_0736 {ECO:0000313|EMBL:BAU23127.1};
OS Caldimicrobium thiodismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23127.1, ECO:0000313|Proteomes:UP000068196};
RN [1] {ECO:0000313|EMBL:BAU23127.1, ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|EMBL:BAU23127.1,
RC ECO:0000313|Proteomes:UP000068196};
RX PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring, and emended description of the genus
RT Caldimicrobium.";
RL Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN [2] {ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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; AP014945; BAU23127.1; -; Genomic_DNA.
DR RefSeq; WP_068513487.1; NZ_AP014945.1.
DR AlphaFoldDB; A0A0U5AGK0; -.
DR STRING; 1653476.THC_0736; -.
DR KEGG; cthi:THC_0736; -.
DR PATRIC; fig|1653476.3.peg.761; -.
DR OrthoDB; 9804453at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000068196; 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; 1.
DR Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
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 InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
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 Reference proteome {ECO:0000313|Proteomes:UP000068196}.
FT DOMAIN 15..397
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 408 AA; 45398 MW; BE19BE07D0D19123 CRC64;
MEGLKKLIKN DAQSKIILIV LDGVGDLPVK DSKTPLELAK TPNLDNLASR SATGLHIPVD
YGITPGSGPG HLGIFGYEPL KYEIGRGILE AVGVGLEVKD TDVAIRGNFA TVKYENGLPI
VIDRRAGRIP TEENKRLIKY LSENIKKIDE AEVILCSGKE HRFSLILRFP YKLSHFFEKI
NDTDPQSTEK PPLLPTGENP EAEKVALIAR KFIEEAAKLL KNEPKANYVL LRGFSVKPAL
EPFPEKFGLK SACIAVYPMY KGLARLVGMD LITFEGESID AEVKTLKEAW QDYDFFFVHI
KKTDSYGEDG NYEGKISVIE EFDRHFLEIV SLNFNVLAIT GDHSTPCIMK SHSWHPVPVL
INSPYCLGGL SLRLTERECL KGELGIFPSF KLMQLLLAHA GRLTKYGA
//
