ID L2F6C2_9GAMM Unreviewed; 528 AA.
AC L2F6C2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=MOMA_07281 {ECO:0000313|EMBL:ELA08346.1};
OS Moraxella macacae 0408225.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA08346.1, ECO:0000313|Proteomes:UP000023795};
RN [1] {ECO:0000313|EMBL:ELA08346.1, ECO:0000313|Proteomes:UP000023795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0408225 {ECO:0000313|EMBL:ELA08346.1,
RC ECO:0000313|Proteomes:UP000023795};
RX PubMed=23409273;
RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT Isolated from a Cynomolgus Macaque with Epistaxis.";
RL Genome Announc. 1:E00188-12(2013).
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:ELA08346.1}.
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DR EMBL; ANIN01000002; ELA08346.1; -; Genomic_DNA.
DR AlphaFoldDB; L2F6C2; -.
DR STRING; 1230338.MOMA_07281; -.
DR PATRIC; fig|1230338.3.peg.1547; -.
DR eggNOG; COG0696; Bacteria.
DR OrthoDB; 9800863at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000023795; 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}; Reference proteome {ECO:0000313|Proteomes:UP000023795}.
FT DOMAIN 5..515
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 82..305
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT ACT_SITE 62
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-1"
FT BINDING 12
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 62
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 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 153..154
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 268..271
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 413
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 417
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 454
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 455
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 473
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 528 AA; 58798 MW; 47F4B77F5C659D2C CRC64;
MKKIPHVLMI LDGFGHREDS KDNAIAHANT PNLDKIYQTY PHGLISGSGE DVGLPDGQFG
NSEVGHMNLG AGRVLYQDST RIHKEIREKT FFDNTVLLEA VQIAKQKSAN VHVMGLLSDG
GVHAHQDHLV AMCELALQQG MDKVFVHAFL DGRDTPPKSA DHYLAIFQKS LDKLNHTYAG
NAYVISVIGR YFAMDRDKRW DRVQQAYDLL TLAKADRVAN SSTDAIQQAY ENDETDEFVK
PTFIQYAEKP NDFGKINDND SVIFMNFRAD RARQISQALV ENDFAGFVRI AQPKISRFVM
LTKYSDELQN NALINTAFMP AKLTNTLGEF LQNHNKTQLR IAETEKYAHV TFFFSGGREQ
EYQGETRILI DSPKVATYDL KPEMSAFEVT EQLQNAIDSG DYDVLIVNYA NGDMVGHTGV
FLATVKAVEA LDSCIGKIAN TVLANHGHLL ITADHGNCEQ MLDYDNGQVH TQHTTELVPL
IYIHENATPS TVSVRQGGKL SDIAPTILAL MGLEKPSEMT GETLLNFN
//
