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Entry: A0A252BWM5_9PROT
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ID   A0A252BWM5_9PROT        Unreviewed;       512 AA.
AC   A0A252BWM5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ORFNames=HK26_10140 {ECO:0000313|EMBL:OUJ13276.1};
OS   Acetobacter okinawensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1076594 {ECO:0000313|EMBL:OUJ13276.1, ECO:0000313|Proteomes:UP000194931};
RN   [1] {ECO:0000313|EMBL:OUJ13276.1, ECO:0000313|Proteomes:UP000194931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DsW_060 {ECO:0000313|EMBL:OUJ13276.1};
RA   Ju J., Zhang J.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:OUJ13276.1}.
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DR   EMBL; JOPJ01000006; OUJ13276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A252BWM5; -.
DR   STRING; 1236501.GCA_000613865_01732; -.
DR   eggNOG; COG0696; Bacteria.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000194931; Unassembled WGS sequence.
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}.
FT   DOMAIN          12..499
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          90..296
FT                   /note="BPG-independent PGAM N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06415"
FT   ACT_SITE        68
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-1"
FT   BINDING         18
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         68
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         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         158..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         259..262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         402
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         406
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         443
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         444
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         462
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   512 AA;  55153 MW;  BE5548409C8FB67F CRC64;
     MPSPRPPHKR TAMLVILDGF GWREDSSDNA VHLARTPSFD RLWHNNPHSF LRTSGEDVGL
     PDGQMGNSEV GHLNIGAGRV VMQELPRIFA AIEDGSLARN PALTDFIAAL KKTGGTCHLM
     GLISAGGVHS HQDHAAALAR IVSDAGVPVA LHLFTDGRDT APRSAANYLQ QLRAALPSAV
     QLATISGRYY AMDRDKRWDR VEKAYNALLS ATGPQAQSPE EVISAAYAQD VSDEFILPTV
     LTGYTGMHDG DGILSFNFRA DRIRQLMDAM LEPDFNGFAR SKVVHFAAAL AMTHYSDALA
     ARMTVLFPPE ELTNLLGEVV AQAGLRQLRM AETEKYPHVT YFMNGGRENL FEGEDRILVP
     SPKVATYDLQ PEMSAPELTD KAVAAIKSGT YDLIVLNFAN PDMVGHTGVL AAAITAVEAV
     DTGLGRIAQA LEEEQGVLLV TADHGNCETM KDPQTGGPHT AHTLNLVPFI VAGSHATKLH
     DGGKLADLAP TLLDIMDLPK PAEMTGQSLL EH
//
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