ID   B4MBT4_DROVI            Unreviewed;       255 AA.
AC   B4MBT4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE            EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
DE            EC=5.4.2.4 {ECO:0000256|RuleBase:RU004511};
GN   Name=Dvir\GJ14508 {ECO:0000313|EMBL:EDW58555.1};
GN   ORFNames=Dvir_GJ14508 {ECO:0000313|EMBL:EDW58555.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW58555.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW58555.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.11; Evidence={ECO:0000256|ARBA:ARBA00000380,
CC         ECO:0000256|RuleBase:RU004511};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC         bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000505,
CC         ECO:0000256|RuleBase:RU004511};
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC       ECO:0000256|RuleBase:RU004511}.
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DR   EMBL; CH940656; EDW58555.1; -; Genomic_DNA.
DR   RefSeq; XP_002058587.1; XM_002058551.2.
DR   AlphaFoldDB; B4MBT4; -.
DR   SMR; B4MBT4; -.
DR   STRING; 7244.B4MBT4; -.
DR   EnsemblMetazoa; FBtr0230433; FBpp0228925; FBgn0201719.
DR   GeneID; 6634953; -.
DR   KEGG; dvi:6634953; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   HOGENOM; CLU_033323_1_1_1; -.
DR   InParanoid; B4MBT4; -.
DR   OMA; RMLPYWY; -.
DR   OrthoDB; 1008469at2759; -.
DR   PhylomeDB; B4MBT4; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0031430; C:M band; IEA:EnsemblMetazoa.
DR   GO; GO:0030018; C:Z disc; IEA:EnsemblMetazoa.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   NCBIfam; TIGR01258; pgm_1; 1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU004511};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU004511};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792}.
FT   ACT_SITE        12
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        90
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         11..18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         90..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         117..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         189..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            188
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   255 AA;  28567 MW;  B1871FC560A6CA0C CRC64;
     MGGKYKIVMV RHGESEWNQK NQFCGWFDAN LSEKGKEEAL AAGKAVKNAG LEFDVAHTSV
     LTRAQVTLAS ILQASGHKEI PIYKTWRLNE RHYGGLTGLN KAETAAKYGE AQVQIWRRSF
     DTPPPPMEPG HPYYDTIVKD PRYAEGPKPE EFPMFESLKL TIERTLPYWN DVIIPQMKEG
     KRILIAAHGN SLRGIVKHLD NLSEDAIMAL NLPTGIPFVY ELDENFKPVV SMQFLGDEET
     VKKAIEAVAA QGKAK
//