GPMI_PROMM
ID GPMI_PROMM Reviewed; 540 AA.
AC Q7V5U5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038};
GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgmI;
GN OrderedLocusNames=PMT_1446;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01038};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01038};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01038}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000255|HAMAP-Rule:MF_01038}.
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DR EMBL; BX548175; CAE21621.1; -; Genomic_DNA.
DR RefSeq; WP_011130814.1; NC_005071.1.
DR AlphaFoldDB; Q7V5U5; -.
DR SMR; Q7V5U5; -.
DR STRING; 74547.PMT_1446; -.
DR EnsemblBacteria; CAE21621; CAE21621; PMT_1446.
DR KEGG; pmt:PMT_1446; -.
DR eggNOG; COG0696; Bacteria.
DR HOGENOM; CLU_026099_2_0_3; -.
DR OMA; FMDGRDT; -.
DR OrthoDB; 338375at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001423; 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; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 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 PANTHER; PTHR31637; PTHR31637; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF64158; SSF64158; 1.
DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..540
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212184"
FT ACT_SITE 74
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 165..166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 268..271
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 408
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 412
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 449
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 450
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 467
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ SEQUENCE 540 AA; 58265 MW; 5CA297C885E6848D CRC64;
MPSSSSGNSR HFSRVAPVVL AILDGWGHRE EVEHNSIRSA ETPIMDALWH AYPHTLIEAS
GAAVGLPDNQ MGNSEVGHLT IGAGRVIRQE LVRISETVQA GRLGQTPALI ALAERLRKSD
GTLHLLGLCS DGGVHSHINH LCGLLHWAAA AGLNKVAVHL ITDGRDTPIQ SASKYLHQIE
DAINASGVGE LASLCGRYWA MDRDHRWERT IRAYEVLTDP NQSISRVTAE DVLSASYANG
TTDEFLEPTR LSNNYFKDGD GLVMFNFRPD RARQLVQALT LPDFDGFPRA NQPSLDVVTF
TQYEHDLPVG VAFPAESLDD LLGQVVSEHG LRQYRTAETE KYPHVTYFMN GGIEQPLAGE
ERHLVPSPRV ATYDLAPAMA ADTLTESCVN AIESGVYSLV VINYANPDMV GHTGVMGAAQ
EAISTVDRCI GRLLDSTGRM GGTLLITADH GNAELMQGSD GQAWTAHTTN PVPVILVEGE
KRKLAGYGND IQLREGGGLA DIAPTLLQLL DLPKPDAMSG LSLIQAIDSP TPSARLPQPV
