PFKA3_PICPA
ID PFKA3_PICPA Reviewed; 351 AA.
AC A7MAS3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit gamma;
DE AltName: Full=ATP-dependent 6-phosphofructokinase;
DE Short=ATP-PFK;
DE Short=Phosphofructokinase 3;
DE AltName: Full=Phosphohexokinase;
GN Name=PFK3;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33; 134-139;
RP 163-177 AND 222-233, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=MH458;
RX PubMed=17522059; DOI=10.1074/jbc.m611547200;
RA Tanneberger K., Kirchberger J., Baer J., Schellenberger W., Rothemund S.,
RA Kamprad M., Otto H., Schoeneberg T., Edelmann A.;
RT "A novel form of 6-phosphofructokinase. Identification and functional
RT relevance of a third type of subunit in Pichia pastoris.";
RL J. Biol. Chem. 282:23687-23697(2007).
RN [2]
RP PARTIAL PROTEIN SEQUENCE OF 2-21, AND SUBUNIT.
RC STRAIN=ATCC 28485 / BCRC 21531 / CBS 704 / DSM 70382 / JCM 3650 / NBRC
RC 10777 / NRRLY-1603;
RX PubMed=12125050; DOI=10.1002/yea.885;
RA Kirchberger J., Baer J., Schellenberger W., Dihazi H., Kopperschlaeger G.;
RT "6-phosphofructokinase from Pichia pastoris: purification, kinetic and
RT molecular characterization of the enzyme.";
RL Yeast 19:933-947(2002).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=19559794; DOI=10.1016/j.jsb.2009.06.014;
RA Benjamin S., Radermacher M., Kirchberger J., Schoeneberg T., Edelmann A.,
RA Ruiz T.;
RT "3D structure of phosphofructokinase from Pichia pastoris: Localization of
RT the novel gamma-subunits.";
RL J. Struct. Biol. 168:345-351(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS).
RX PubMed=20833871; DOI=10.1096/fj.10-163865;
RA Straeter N., Marek S., Kuettner E.B., Kloos M., Keim A., Brueser A.,
RA Kirchberger J., Schoeneberg T.;
RT "Molecular architecture and structural basis of allosteric regulation of
RT eukaryotic phosphofructokinases.";
RL FASEB J. 25:89-98(2011).
CC -!- FUNCTION: Structural subunit of pyrophosphate--fructose 6-phosphate 1-
CC phosphotransferase. Not required for catalytic activity. Fine-tunes
CC allosteric regulation of the ATP-PFK by ATP, fructose 2,6-bisphosphate
CC and AMP. {ECO:0000269|PubMed:17522059}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC -!- SUBUNIT: Heterododecamer of 4 alpha, 4 beta and 4 gamma chains. The
CC gamma chain bridges the N-terminal halves of the alpha and beta
CC subunits. {ECO:0000269|PubMed:12125050, ECO:0000269|PubMed:17522059,
CC ECO:0000269|PubMed:19559794}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17522059}.
CC -!- MISCELLANEOUS: This subunit is only found in some Pichia species.
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DR EMBL; AY686600; AAU05772.1; -; Genomic_DNA.
DR PDB; 3OPY; X-ray; 3.05 A; I/J/K/L=1-351.
DR PDBsum; 3OPY; -.
DR AlphaFoldDB; A7MAS3; -.
DR SMR; A7MAS3; -.
DR SABIO-RK; A7MAS3; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11687; PpPFK_gamma; 1.
DR Gene3D; 3.40.50.11920; -; 1.
DR InterPro; IPR033785; PpPFK_gamma.
DR InterPro; IPR038615; PpPFK_gamma_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17522059"
FT CHAIN 2..351
FT /note="ATP-dependent 6-phosphofructokinase subunit gamma"
FT /id="PRO_0000429725"
FT CONFLICT 21
FT /note="G -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 269..278
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 297..311
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 341..349
FT /evidence="ECO:0007829|PDB:3OPY"
SQ SEQUENCE 351 AA; 40796 MW; CC66BE17B4D878F5 CRC64;
MVTKDSIIRD LERENVGPEF GEFLNTLQTD LNSEKPPIEQ VKSQLETHFN LAHETQEFSR
KNDNAPVDKL LTNYYNNYEV NVLEFVLQMG FSRDLSIPLN VWFVLDMISQ LSTSKQDLPL
DYYLVLNNSQ TGKYSDFVRY LIYEAVGAEI HCFEQGSMPE QYRSSRWEDK VKGPALANRG
PIRGNVGAGD RKITFHLLCK KTARMILVGD DRETDFEMSD RSFVTLLLDY YQRVGTTKKI
DLLLLTNNFD TNMNNKLQQL KILESLNMLK SNCYVLDYQI TVDQVTANFN SYVEGIPAFR
RHEIANFLKK RKTPKNADEL IFKYVGRWNI CYQKKFHQGN ISIHQISGYL D
