ID W7KLM5_9CREN Unreviewed; 415 AA.
AC W7KLM5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=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=ASUL_01565 {ECO:0000313|EMBL:EWG08300.1}, TQ35_00930
GN {ECO:0000313|EMBL:KJR79588.1};
OS Candidatus Aramenus sulfurataquae.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Aramenus.
OX NCBI_TaxID=1326980 {ECO:0000313|EMBL:EWG08300.1, ECO:0000313|Proteomes:UP000054284};
RN [1] {ECO:0000313|EMBL:EWG08300.1, ECO:0000313|Proteomes:UP000054284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1-illumnia {ECO:0000313|EMBL:EWG08300.1};
RX PubMed=24604657;
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Draft Genome Sequence of the Sulfolobales Archaeon AZ1, Obtained through
RT Metagenomic Analysis of a Mexican Hot Spring.";
RL Genome Announc. 2:e00164-14(2014).
RN [2] {ECO:0000313|EMBL:KJR79588.1, ECO:0000313|Proteomes:UP000053480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1-454 {ECO:0000313|EMBL:KJR79588.1};
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-2015) 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|ARBA:ARBA00004798,
CC ECO:0000256|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWG08300.1}.
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DR EMBL; ASRH01000001; EWG08300.1; -; Genomic_DNA.
DR EMBL; JZWS01000003; KJR79588.1; -; Genomic_DNA.
DR AlphaFoldDB; W7KLM5; -.
DR PATRIC; fig|1326980.6.peg.308; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000053480; Unassembled WGS sequence.
DR Proteomes; UP000054284; Unassembled WGS sequence.
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_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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054284}.
FT DOMAIN 5..405
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT COILED 112..139
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 415 AA; 45291 MW; 1DCFEFDF2F4C2C61 CRC64;
MRRHKVLLII ADGLGDRQVK ALGNRTPLEA ADKPNIRSLL RSSLVGLMNP ISPGVVPGSD
TSHLAIFGLD PRKYYSGRGS FEALGSGVEL AEGDVSFRGN FATVDSDLRV VDRRAGRNIE
EAEDLVRELN SKIGEINGVK VRFYKGTEHR VSVVISGEGL SDKVSDTDPH EVGLKVKESK
PLEESQEAAR TADLLNKLTR RIYEVLSSSE ANKLRVQRNK PPANIVLLRG AAKYKELPKL
RDYTGLNAAA VSATPLIKGI CKAIGMEVIT PKGATGGIDT NYDAKANAVI DFLKSDKYDL
VFLHIKATDA ASHDGKAEEK VRAIEKIDYV IGRILDNYSS ELVIAFTGDH ATPVELKEHA
GDPVPFFLYV PENIIPDGVS DFNEREARKG TIRISGLDVM NILLNYSNRA TKYGA
//
