ID GPMA_ARTCA Reviewed; 248 AA.
AC B8HCQ9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
DE Short=BPG-dependent PGAM;
DE Short=PGAM;
DE Short=Phosphoglyceromutase;
DE Short=dPGM;
DE EC=5.4.2.1;
GN Name=gpmA; OrderedLocusNames=Achl_0847;
OS Arthrobacter chlorophenolicus (strain A6 / ATCC 700700 / DSM 12829 /
OS JCM 12360).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micrococcineae; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A6 / ATCC 700700 / DSM 12829 / JCM 12360;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus
RT A6.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC 3-phosphoglycerate (By similarity).
CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily.
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DR EMBL; CP001341; ACL38842.1; -; Genomic_DNA.
DR RefSeq; YP_002486931.1; NC_011886.1.
DR ProteinModelPortal; B8HCQ9; -.
DR SMR; B8HCQ9; 2-235.
DR STRING; 452863.Achl_0847; -.
DR EnsemblBacteria; ACL38842; ACL38842; Achl_0847.
DR GeneID; 7292284; -.
DR KEGG; ach:Achl_0847; -.
DR PATRIC; 20988193; VBIArtChl38304_1503.
DR eggNOG; COG0588; -.
DR HOGENOM; HOG000221682; -.
DR KO; K01834; -.
DR OMA; GQSDWNL; -.
DR ProtClustDB; PRK14120; -.
DR BioCyc; ACHL452863:GH1A-861-MONOMER; -.
DR UniPathway; UPA00109; UER00186.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:HAMAP.
DR GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR HAMAP; MF_01039; PGAM_GpmA; 1; -.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Glycolysis; Isomerase.
FT CHAIN 1 248 2,3-bisphosphoglycerate-dependent
FT phosphoglycerate mutase.
FT /FTId=PRO_1000149496.
FT ACT_SITE 10 10 Tele-phosphohistidine intermediate (By
FT similarity).
FT ACT_SITE 182 182 By similarity.
FT SITE 61 61 Interaction with carboxyl group of
FT phosphoglycerates (By similarity).
SQ SEQUENCE 248 AA; 27710 MW; 2CCD15883A920EBC CRC64;
MTYKLILLRH GHSEWNAKNL FTGWVDVDLN DQGRAEAARG GELLVENNIL PDVLYTSLLK
RAINTANIAL DKADRGWIPV KRDWRLNERH YGALQGKDKA QTLAEYGEEQ FMEWRRSYDT
PPPPLDDNSE FSQAHDPRYA DLGDALPRTE CLKDVLVRIL PYWESDIKAD LKAGKTVLVT
AHGNSLRALV KHLDGISDEA IAGLNIPTGI PLVYDLDDDF QPVKPGGTYL DPEAAEQAIL
AVANQGKK
//
