ID   PGAM4_PANTR             Reviewed;         254 AA.
AC   Q8MKE8; Q2VIN5;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Probable phosphoglycerate mutase 4;
DE            EC=5.4.2.1;
DE            EC=5.4.2.4;
DE            EC=3.1.3.13;
GN   Name=PGAM4; Synonyms=PGAM3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21959328; PubMed=11961099;
RA   Betran E., Wang W., Jin L., Long M.;
RT   "Evolution of the phosphoglycerate mutase processed gene in human and
RT   chimpanzee revealing the origin of a new primate gene.";
RL   Mol. Biol. Evol. 19:654-663(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA   Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT   "Emergence of young human genes after a burst of retroposition in
RT   primates.";
RL   PLoS Biol. 3:1970-1979(2005).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-
CC       bisphospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H(2)O = 3-
CC       phospho-D-glycerate + phosphate.
CC   -!- MISCELLANEOUS: This is the product of a processed gene created by
CC       retroposition from mRNA of an expressed gene. This gene seems to
CC       be expressed.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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DR   EMBL; AF465746; AAM27297.1; -; Genomic_DNA.
DR   EMBL; DQ120648; ABB92433.1; -; Genomic_DNA.
DR   RefSeq; NP_001009163.1; -.
DR   HSSP; P31217; 1E58.
DR   SMR; Q8MKE8; 2-246.
DR   GeneID; 494122; -.
DR   KEGG; ptr:494122; -.
DR   HOVERGEN; Q8MKE8; -.
DR   OMA; Q8MKE8; RVLPYWY.
DR   BRENDA; 3.1.3.13; 264977.
DR   BRENDA; 5.4.2.1; 264977.
DR   BRENDA; 5.4.2.4; 264977.
DR   GO; GO:0004083; F:2,3-bisphospho-D-glycerate 2-phosphohydrola...; IEA:EC.
DR   GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:EC.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001345; PG/BPGM_mutase.
DR   InterPro; IPR013078; PG_mutase.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; Phosphogly_mut1; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein.
FT   CHAIN         1    254       Probable phosphoglycerate mutase 4.
FT                                /FTId=PRO_0000179833.
FT   COMPBIAS    122    131       Pro-rich.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    186    186       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
FT   MOD_RES      92     92       Phosphotyrosine (By similarity).
FT   MOD_RES     106    106       N6-acetyllysine (By similarity).
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     119    119       Phosphotyrosine (By similarity).
FT   MOD_RES     133    133       Phosphotyrosine (By similarity).
SQ   SEQUENCE   254 AA;  28809 MW;  0F073CDE449EDD39 CRC64;
     MAAYKLVLIR HGESTWNLEN RFSCWYDADL SPAGHEEAKR GGQALRDAGY EFDICLTSVQ
     KRVIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTALNK AETAAKHGEA QVKIWRRSYD
     VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSYESPKDTI ARALPFWNEE IVPQIKEGKR
     VLIAAHGNSL QGIAKHVEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVC
     KAMEAVAAQG KAKK
//