ID KPYK_EMENI Reviewed; 526 AA.
AC P22360; C8VF86; Q5B2M0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-APR-2013, entry version 99.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pkiA; Synonyms=pki; ORFNames=AN5210;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS 194 / M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WG096;
RX PubMed=3072099; DOI=10.1007/BF00434080;
RA de Graaff L., Visser J.;
RT "Structure of the Aspergillus nidulans pyruvate kinase gene.";
RL Curr. Genet. 14:553-560(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a
RT community effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC -!- COFACTOR: Magnesium.
CC -!- COFACTOR: Potassium.
CC -!- ENZYME REGULATION: Regulated by phosphoenolpyruvate substrate and
CC allosteric effectors such as fructose 1,6 diphosphate and
CC magnesium.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR EMBL; M36918; AAA33320.1; -; Genomic_DNA.
DR EMBL; AACD01000089; EAA62391.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81089.1; -; Genomic_DNA.
DR PIR; S27364; S27364.
DR RefSeq; XP_662814.1; XM_657722.1.
DR ProteinModelPortal; P22360; -.
DR SMR; P22360; 31-515.
DR STRING; 162425.CADANIAP00003208; -.
DR PRIDE; P22360; -.
DR EnsemblFungi; CADANIAT00003208; CADANIAP00003208; CADANIAG00003208.
DR GeneID; 2871501; -.
DR KEGG; ani:AN5210.2; -.
DR eggNOG; COG0469; -.
DR HOGENOM; HOG000021559; -.
DR KO; K00873; -.
DR OMA; NSGYTAR; -.
DR OrthoDB; EOG43XZC1; -.
DR UniPathway; UPA00109; UER00188.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:EC.
DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 2.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom.
DR InterPro; IPR015794; Pyrv_Knase_a/b.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; PK_B_barrel_like; 1.
DR SUPFAM; SSF52935; Pyruvate_kinase; 1.
DR SUPFAM; SSF51621; Pyrv/PenolPyrv_Kinase_cat; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Complete proteome; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1 526 Pyruvate kinase.
FT /FTId=PRO_0000112113.
FT METAL 65 65 Potassium (By similarity).
FT METAL 67 67 Potassium (By similarity).
FT METAL 98 98 Potassium (By similarity).
FT METAL 99 99 Potassium; via carbonyl oxygen (By
FT similarity).
FT METAL 256 256 Magnesium (Potential).
FT METAL 280 280 Magnesium (By similarity).
FT BINDING 63 63 Substrate (By similarity).
FT BINDING 279 279 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 280 280 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 312 312 Substrate (By similarity).
FT BINDING 351 351 ADP (Potential).
FT SITE 254 254 Transition state stabilizer (By
FT similarity).
FT MOD_RES 36 36 Phosphoserine (Potential).
FT CONFLICT 88 88 Q -> A (in Ref. 1; AAA33320).
SQ SEQUENCE 526 AA; 58133 MW; BCD3A6F35F5D28B2 CRC64;
MAASSSLDHL SNRMKLEWHS KLNTEMVPAK NFRRTSIICT IGPKTNSVEK INALRRAGLN
VVRMNFSHGS YEYHQSVIDH AREAEKQQAG RPVAIALDTK GPEIRTGNTV GDKDIPIKAG
HEMNISTDEQ YATASDDQNM YVDYKNITKV ISAGKLIYVD DGILSFEVLE VVDDKTLRVR
CLNNGNISSR KGVNLPGTDV DLPALSEKDI SDLKFGVKNK VDMVFASFIR RGSDIRHIRE
VLGEEGREIQ IIAKIENQQG VNNFDEILEE TDGVMVARGD LGIEIPAPKV FIAQKMMIAK
CNIKGKPVIC ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA KGNYPCEAVT
MMSETCLLAE VAIPHFNVFD ELRNLAPRPT DTVESIAMAA VSASLELNAG AIVVLTTSGN
TARMISKYRP VCPIIMVSRN PAATRYSHLY RGVWPFYFPE KKPDFNVKIW QEDVDRRLKW
GINHGLKLGI INKGDNIVCV QGWRGGMGHT NTVRVVPAEE NLGLSE
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