ID A0A0Q8ZU54_9FLAO Unreviewed; 505 AA.
AC A0A0Q8ZU54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=ASE21_15780 {ECO:0000313|EMBL:KRD08154.1};
OS Flavobacterium sp. Root901.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736605 {ECO:0000313|EMBL:KRD08154.1, ECO:0000313|Proteomes:UP000051400};
RN [1] {ECO:0000313|EMBL:KRD08154.1, ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|EMBL:KRD08154.1,
RC ECO:0000313|Proteomes:UP000051400};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRD08154.1}.
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DR EMBL; LMJB01000008; KRD08154.1; -; Genomic_DNA.
DR RefSeq; WP_057123720.1; NZ_LMJB01000008.1.
DR AlphaFoldDB; A0A0Q8ZU54; -.
DR STRING; 1736605.ASE21_15780; -.
DR OrthoDB; 9800863at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000051400; 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..494
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; 55861 MW; 4FBDE91F2B6CC9CA CRC64;
MNKKVILMIL DGWGKSPDPK VSAIDNANVP FINSLYKNYP SAQLRTDGLN VGLPEGQMGN
SEVGHMNLGA GRIVYQDLAK INLAVAHKTL AKEQVLIDAF TYAKDNNKKV HFLGLVSDGG
VHSHTSHLRG LIDASQEYGL DQVYIHAFTD GRDVDPKSGA KYIHDLDEYI KDTPVKIASI
IGRYYAMDRD KRWERVKLAY DLVVNGVGTP SKNAVASVLD SYAKDVTDEF IEPVVVVDQN
EKPLATIVEG DVVIFFNFRT DRGRELTEAL SQHDFHEQNM HKLNLYYVTL TNYDETYQNV
KVVYNKDNIT ETLGEVLEKA GKKQIRIAET EKYPHVTFFF SGGRETPFEG ESRILRNSPK
VATYDLQPEM SAYELADALV PELNKGDVDF VCLNFANGDM VGHTGIMEAA IRACEAVDAC
AKKVIEAALA NDYTTIVIAD HGNCETMINP DGSPNTAHTT NPVPIILVDK QLKNIQDGVL
GDIAPTILEL MGVQQPNAMT CHSLL
//
