ID E0UPM2_SULAO Unreviewed; 491 AA.
AC E0UPM2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01038};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE Short=iPGM {ECO:0000256|HAMAP-Rule:MF_01038};
DE EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01038};
GN Name=gpmI {ECO:0000256|HAMAP-Rule:MF_01038};
GN OrderedLocusNames=Saut_0565 {ECO:0000313|EMBL:ADN08614.1};
OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS OK10).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN08614.1, ECO:0000313|Proteomes:UP000007803};
RN [1] {ECO:0000313|EMBL:ADN08614.1, ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX PubMed=21304749;
RA Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10).";
RL Stand. Genomic Sci. 3:194-202(2010).
RN [2] {ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX DOI=10.4056/sigs.1173118;
RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10T).";
RL Stand. Genomic Sci. 3:194-202(2010).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038}.
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_01038};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01038};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01038};
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_01038}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000256|ARBA:ARBA00008819, ECO:0000256|HAMAP-
CC Rule:MF_01038}.
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DR EMBL; CP002205; ADN08614.1; -; Genomic_DNA.
DR RefSeq; WP_013326370.1; NC_014506.1.
DR AlphaFoldDB; E0UPM2; -.
DR STRING; 563040.Saut_0565; -.
DR KEGG; sua:Saut_0565; -.
DR eggNOG; COG0696; Bacteria.
DR HOGENOM; CLU_026099_2_0_7; -.
DR OrthoDB; 9800863at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000007803; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR HAMAP; MF_01038; GpmI; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 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_01038};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01038};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01038}; Reference proteome {ECO:0000313|Proteomes:UP000007803}.
FT DOMAIN 3..481
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 81..284
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT ACT_SITE 61
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-1"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 147..148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 248..251
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 386
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 390
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 427
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 428
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
SQ SEQUENCE 491 AA; 55081 MW; 6B7F5E5F39C69678 CRC64;
MSKKAILVIT DGIGYCSKTE HNAFYNANKP TYDKLFSEVP HALIDTFGLS VGLPEGQMGN
SEVGHMSIGS GRVLYQDLVK ISLALQDGSL EQNEVLQDLF KKSDRLHLIG LMSDGGVHSH
IDHFMGIADI AAKNGKTVFL HLITDGRDVS PTSAQKYLEE VRKHVNENVK IASISGRFYA
MDRDNRWERI KRAYDAIVNA EPKTDMTPES YIGHSYSLGE TDEFVEPTAF KDYNGMQEGD
SVLTINFRSD RMREMVRAIA DENFTEFERR VQDVNLATIT EYDKSFPYPV MFRKDVPKNT
LAEVIANAGL RQLHTAETEK YAHVTFFLNG GIDEPYENET RVLIPSPNVK TYDMKPEMSA
NEVCEAVLEA MDADYDFVVV NFANGDMVGH TGDFEAAKKA VEAVDEQLGK IYEKAKEKEY
AFVLTSDHGN CEEMRDEYDN VLTNHTVGKV WCFVDAKGVK KVKTGGLNNI APTVLKLMEL
EIPVEMDESL V
//
