GPMI_AGRFC
ID GPMI_AGRFC Reviewed; 505 AA.
AC Q8UAA5;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=pgm;
GN OrderedLocusNames=Atu3469; ORFNames=AGR_L_2721;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007870; AAK89925.1; -; Genomic_DNA.
DR PIR; AD2983; AD2983.
DR PIR; C98300; C98300.
DR RefSeq; NP_357140.1; NC_003063.2.
DR RefSeq; WP_010973066.1; NC_003063.2.
DR AlphaFoldDB; Q8UAA5; -.
DR SMR; Q8UAA5; -.
DR STRING; 176299.Atu3469; -.
DR EnsemblBacteria; AAK89925; AAK89925; Atu3469.
DR KEGG; atu:Atu3469; -.
DR PATRIC; fig|176299.10.peg.3308; -.
DR eggNOG; COG0696; Bacteria.
DR HOGENOM; CLU_026099_2_0_5; -.
DR OMA; FMDGRDT; -.
DR PhylomeDB; Q8UAA5; -.
DR BioCyc; AGRO:ATU3469-MON; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000813; Chromosome linear.
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..505
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212116"
FT ACT_SITE 63
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 153..154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 254..257
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 395
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 399
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 437
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 455
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ SEQUENCE 505 AA; 53638 MW; B310AA3CAD31B6DC CRC64;
MRTPKPVVLT ILDGWGLNED TSSNAPVLAN TPTMDRLFAT CPNATLTTFG PNVGLPTGQM
GNSEVGHTNI GAGRIVAMDL GQIDLAIEDG SFFRNAAMLD FAATVKAAGG VAHLMCVVSD
GGVHGHILHG QAAVKLMVSH GLKVVVHAIT DGRDVAPQSA EDFVAALVAS LPQGASIGTV
IGRYYAMDRD NRWERVEKAY DAMVLGKGEH ARDAVSAVAQ SYANKVTDEF ILPTVIDGYE
GFKAGDGLFC LNFRADRARE ILLAIGADDF DGFAREKPVL SALLGMVEYS TRHSDFMTTA
YPKRDIVNTL GAWVAKQGLT QFRLAETEKY PHVTFFLNGG KEEPEVGEDR FMPKSPKVAT
YDLQPEMSAA EVTEKFVEVI GKGYDLIVTN YANPDMVGHT GDLQAAIKAC EAVDRGLGAV
VAALEKVGGA MLVIADHGNC ETMVDPVTGG PHTAHTTNPV PVILFGGPEG AKVHDGILAD
VAPTLLQLMN VPLPPEMTGK SLIDL
