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Database: UniProt
Entry: A0A1I1Z1A2_9FLAO
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ID   A0A1I1Z1A2_9FLAO        Unreviewed;       505 AA.
AC   A0A1I1Z1A2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=SAMN04488131_101208 {ECO:0000313|EMBL:SFE25342.1};
OS   Flavobacterium xueshanense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=935223 {ECO:0000313|EMBL:SFE25342.1, ECO:0000313|Proteomes:UP000198596};
RN   [1] {ECO:0000313|EMBL:SFE25342.1, ECO:0000313|Proteomes:UP000198596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9227 {ECO:0000313|EMBL:SFE25342.1,
RC   ECO:0000313|Proteomes:UP000198596};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FONQ01000001; SFE25342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1Z1A2; -.
DR   STRING; 935223.SAMN04488131_101208; -.
DR   OrthoDB; 9800863at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000198596; 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          3..495
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          81..295
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         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         152..153
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         189
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         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         399
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         403
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         440
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         441
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         458
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   505 AA;  56535 MW;  BE71D74D4685E5A9 CRC64;
     MNKKVILMIL DGWGKSPDPK ISAIDNSNVP FINSLYRNYP SAQLRTDGLN VGLPDGQMGN
     SEVGHMNLGA GRIVYQDLAK INLAVAHDTL AKEQVLVDAF TYARINNKKV HFLGLVSDGG
     VHSHTSHLRG LIDATQQHGL QNVFVHAFTD GRDVDPKSGK HYIQDLQDYI ANTTVKLASV
     VGRYYAMDRD RRWERVKLAY DLLVNGIGTH SRNAVANIEE SYEVNVTDEF IHPMVMVDEY
     DQPLATIEED DVVIFFNFRT DRGRELTEVL TQMDCHEQNM HKLNLYYVTL TNYDETYKNV
     KVVYNKDNIT ETLGEVLEKA HKKQIRIAET EKYPHVTFFF SGGRERPFIG ESRILKNSPK
     VATYDLQPEM SAFELTAALI PELEKEEVDF VCLNFANGDM VGHTGIMSAA IKACEAVDKC
     VERVITTALA HNYTTIVIAD HGNCETMINP DGSPNTAHTT NPVPMILVDN DLRTIHDGVL
     GDIAPTILEL MGIEKPEAMT CHSLL
//
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