(data stored in ACNUC7421 zone)

SWISSPROT: A0KF05_AERHH

ID   A0KF05_AERHH            Unreviewed;       574 AA.
AC   A0KF05;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
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   ECO:0000313|EMBL:ABK36201.1};
GN   OrderedLocusNames=AHA_0293 {ECO:0000313|EMBL:ABK36201.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK36201.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK36201.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038,
CC       ECO:0000256|SAAS:SAAS00978404}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = 3-phospho-D-glycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.12; Evidence={ECO:0000256|HAMAP-Rule:MF_01038,
CC         ECO:0000256|SAAS:SAAS01115646};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         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|HAMAP-
CC       Rule:MF_01038, ECO:0000256|SAAS:SAAS00850947}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01038,
CC       ECO:0000256|SAAS:SAAS00850933}.
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DR   EMBL; CP000462; ABK36201.1; -; Genomic_DNA.
DR   RefSeq; WP_011704299.1; NC_008570.1.
DR   RefSeq; YP_854823.1; NC_008570.1.
DR   STRING; 380703.AHA_0293; -.
DR   EnsemblBacteria; ABK36201; ABK36201; AHA_0293.
DR   GeneID; 4490451; -.
DR   KEGG; aha:AHA_0293; -.
DR   PATRIC; fig|380703.7.peg.281; -.
DR   eggNOG; ENOG4105CJI; Bacteria.
DR   eggNOG; COG0696; LUCA.
DR   HOGENOM; HOG000223664; -.
DR   KO; K15633; -.
DR   OMA; FMDGRDT; -.
DR   BioCyc; AHYD380703:G1G7B-294-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000756; 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;
DR   PRODOM; A0KF05.
DR   SWISS-2DPAGE; A0KF05.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00850939};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00850936, ECO:0000313|EMBL:ABK36201.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00241368};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00241382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN       71    559       Metalloenzyme. {ECO:0000259|Pfam:
FT                                PF01676}.
FT   DOMAIN      149    360       iPGM_N. {ECO:0000259|Pfam:PF06415}.
FT   REGION      220    221       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01038}.
FT   REGION      324    327       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01038}.
FT   ACT_SITE    129    129       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01038}.
FT   METAL        79     79       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       129    129       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       464    464       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       468    468       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       505    505       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       506    506       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       524    524       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     190    190       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     252    252       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     258    258       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     397    397       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
SQ   SEQUENCE   574 AA;  62290 MW;  FB9B9AE29DDA66C4 CRC64;
     MAFGPLGRGF VEWCDKPATK KKQLGNSVRP PPDGAWLSGD YFGRCSNITL VSLPAIHSYP
     RGHSLMSTAK KPLVLVIMDG WGYSTKQEHN AVAAAKTPNL DRLARDYTST LISGSGLDVG
     LPDGQMGNSE VGHVNIGAGR IVYQELTRIS KDIQDGDFFQ NVELAKAVDA AVTKGKAVHI
     MGLMSPGGVH SHEEHIMGMI EMAAKRGAEQ IYFHAFLDGR DVPPRSAQSS IEQFDALFAR
     LGKGRFASMI GRYYAMDRDN RWDRVQQAYD LMTQGKGEFT ADSASEALAA AYARDENDEF
     VKATRIGAAA PMQDGDALIF MNFRADRARE ITRAFVDSDF TGFARTATPA LNFVMLTEYA
     ADIKTACAYP PTALVNTLGE WLAKQGKTQL RISETEKYAH VTFFFNGGEE ACFTGEDREI
     VASPKVATYD LQPEMSSEEL TDKLVGAIKS GKYDVIICNY PNGDMVGHTG VFDAAVKACE
     AVDHCIGRVT DALAEVGGEC LITADHGNAE KMMDEETGQA HTAHTNLPVP LIYFGRKAEV
     AEGGKLSDLA PTMLTLMGLP VPPEMTGKPL MILK
//

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