ID A8LZG5_SALAI Unreviewed; 255 AA.
AC A8LZG5;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 01-MAY-2013, entry version 37.
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=Sare_0402;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micromonosporineae; Micromonosporaceae; Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S.,
RA Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) 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; CP000850; ABV96331.1; -; Genomic_DNA.
DR RefSeq; YP_001535322.1; NC_009953.1.
DR ProteinModelPortal; A8LZG5; -.
DR SMR; A8LZG5; 10-243.
DR STRING; 391037.Sare_0402; -.
DR EnsemblBacteria; ABV96331; ABV96331; Sare_0402.
DR GeneID; 5703795; -.
DR KEGG; saq:Sare_0402; -.
DR PATRIC; 23429239; VBISalAre38676_0409.
DR eggNOG; COG0588; -.
DR HOGENOM; HOG000221682; -.
DR KO; K01834; -.
DR OMA; GQSDWNL; -.
DR ProtClustDB; CLSK968601; -.
DR BioCyc; SARE391037:GH66-465-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; IPR001345; PG/BPGM_mutase_AS.
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; 1.
PE 3: Inferred from homology;
KW Complete proteome; Glycolysis; Isomerase.
FT ACT_SITE 17 17 Tele-phosphohistidine intermediate (By
FT similarity).
FT ACT_SITE 190 190 By similarity.
FT SITE 68 68 Interaction with carboxyl group of
FT phosphoglycerates (By similarity).
SQ SEQUENCE 255 AA; 28771 MW; FE9B06E513DF3FCC CRC64;
MTASEGPTVG TLVLLRHGES DWNAKNLFTG WVDVDLTGKG ETEARRGGEL LREHNLLPDV
VHTSLLRRAI RTAELALETA ERNWIAVRRS WRLNERHYGA LQGKNKKQTL DEYGEEQFML
WRRSYDTPPP PIADDDEWSQ VGDPRYRLLP TELMPRTECL KDVVERMLPY WYDSIVPDIL
AGRTVLVAAH GNSLRALVKH LDQISDEAIA KLNIPTGIPL RYDLDPQLRP MTLGGTYLDP
TAARDAAAAV ANQGR
//
