PCKGM_CHICK
ID PCKGM_CHICK Reviewed; 641 AA.
AC P21642;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP], mitochondrial;
DE Short=PEPCK-M;
DE EC=4.1.1.32;
DE Flags: Precursor;
GN Name=PCK2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=2110163; DOI=10.1016/s0021-9258(19)39115-x;
RA Weldon S.L., Rando A., Matathias A.S., Hod Y., Kalonick P.A., Savon S.,
RA Cook J.S., Hanson R.W.;
RT "Mitochondrial phosphoenolpyruvate carboxykinase from the chicken.
RT Comparison of the cDNA and protein sequences with the cytosolic isozyme.";
RL J. Biol. Chem. 265:7308-7317(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 34-641 IN COMPLEX WITH MANGANESE;
RP GTP AND SUBSTRATE ANALOG, SEQUENCE REVISION, COFACTOR, SUBUNIT, AND ACTIVE
RP SITE.
RX PubMed=16819824; DOI=10.1021/bi060269g;
RA Holyoak T., Sullivan S.M., Nowak T.;
RT "Structural insights into the mechanism of PEPCK catalysis.";
RL Biochemistry 45:8254-8263(2006).
CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC pathway that produces glucose from lactate and other precursors derived
CC from the citric acid cycle. Facilitates the recycling of lactate carbon
CC in the liver.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16819824};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:16819824};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16819824}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Present in liver and kidney.
CC {ECO:0000269|PubMed:2110163}.
CC -!- INDUCTION: Appears to be constitutively expressed.
CC -!- MISCELLANEOUS: In eukaryotes there are two isozymes: a cytoplasmic one
CC and a mitochondrial one. In birds, PEPCK-M is the sole form of hepatic
CC PEPCK, but it constitutes 60% of the enzyme in the kidney.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000305}.
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DR EMBL; J05419; AAA49006.1; -; mRNA.
DR PIR; A35191; QYCHGM.
DR RefSeq; NP_990801.1; NM_205470.1.
DR PDB; 2FAF; X-ray; 1.70 A; A/B=34-641.
DR PDB; 2FAH; X-ray; 2.09 A; A/B/C/D=34-128, A/B/C/D=130-641.
DR PDB; 2QZY; X-ray; 1.90 A; A/B=34-641.
DR PDBsum; 2FAF; -.
DR PDBsum; 2FAH; -.
DR PDBsum; 2QZY; -.
DR AlphaFoldDB; P21642; -.
DR SMR; P21642; -.
DR STRING; 9031.ENSGALP00000015626; -.
DR GeneID; 396457; -.
DR KEGG; gga:396457; -.
DR CTD; 5106; -.
DR VEuPathDB; HostDB:geneid_396457; -.
DR eggNOG; KOG3749; Eukaryota.
DR InParanoid; P21642; -.
DR OrthoDB; 286671at2759; -.
DR PhylomeDB; P21642; -.
DR BRENDA; 4.1.1.32; 1306.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR SABIO-RK; P21642; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P21642; -.
DR PRO; PR:P21642; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IBA:GO_Central.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:AgBase.
DR GO; GO:0071361; P:cellular response to ethanol; IDA:AgBase.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:AgBase.
DR GO; GO:0030703; P:eggshell formation; IMP:AgBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:AgBase.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IEP:AgBase.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0019661; P:glucose catabolic process to lactate via pyruvate; TAS:AgBase.
DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IDA:AgBase.
DR GO; GO:0070365; P:hepatocyte differentiation; IEP:AgBase.
DR GO; GO:0006089; P:lactate metabolic process; IDA:AgBase.
DR GO; GO:0019516; P:lactate oxidation; TAS:AgBase.
DR GO; GO:0018991; P:oviposition; TAS:AgBase.
DR GO; GO:0019543; P:propionate catabolic process; IDA:AgBase.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:AgBase.
DR GO; GO:0006111; P:regulation of gluconeogenesis; TAS:AgBase.
DR GO; GO:0050792; P:regulation of viral process; IGI:AgBase.
DR GO; GO:0051591; P:response to cAMP; IDA:AgBase.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IDA:AgBase.
DR GO; GO:0007296; P:vitellogenesis; IMP:AgBase.
DR CDD; cd00819; PEPCK_GTP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR HAMAP; MF_00452; PEPCK_GTP; 1.
DR InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008209; PEP_carboxykinase_GTP.
DR InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PTHR11561; 1.
DR Pfam; PF00821; PEPCK_GTP; 1.
DR Pfam; PF17297; PEPCK_N; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Direct protein sequencing; Gluconeogenesis;
KW GTP-binding; Lyase; Manganese; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT CHAIN 34..641
FT /note="Phosphoenolpyruvate carboxykinase [GTP],
FT mitochondrial"
FT /id="PRO_0000023570"
FT ACT_SITE 307
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 254..256
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 283
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 306..311
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 330
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 422..424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 424
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16819824"
FT BINDING 549..552
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16819824"
FT CONFLICT 107
FT /note="E -> Q (in Ref. 1; AAA49006)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..130
FT /note="GP -> S (in Ref. 1; AAA49006)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="P -> R (in Ref. 1; AAA49006)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="R -> A (in Ref. 1; AAA49006)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="E -> R (in Ref. 1; AAA49006)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="R -> S (in Ref. 1; AAA49006)"
FT /evidence="ECO:0000305"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2FAH"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2FAH"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:2FAF"
FT TURN 151..156
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2FAH"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:2FAF"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:2FAF"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 445..454
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 469..477
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2FAH"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:2FAH"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:2FAH"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 509..519
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 529..535
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 552..563
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:2FAF"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:2FAF"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:2QZY"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 601..618
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:2FAF"
FT HELIX 625..639
FT /evidence="ECO:0007829|PDB:2FAF"
SQ SEQUENCE 641 AA; 71106 MW; A5C2BA63C659E633 CRC64;
MFWLRGGAQS CRGGETEDRM QRGMWGVGLA RRRLSTSLSA LPAAARDFVE EAVRLCRPRE
VLLCDGSEEE GKELLRGLQD DGVLHPLPKY DNCWLARTDP RDVARVESKT VLVTPEQSDA
VPPPPPSGGP PQLGNWMSPN AFQAAVQERF PGCMAGRPLY VIPFSMGPPT SPLAKLGVQV
TDSPYVVLSM RIMTRVGPAV LQRLDDDFVR CLHSVGRPLP LTEPLVSSWP CDRSPVLVAH
IPSERRIVSF GSGYGGNSLL GKKCFALRIA SRMAQQQGWL AEHMLILGVT SPSGEKRYMA
AAFPSACGKT NLAMMTPSLP GWRIHCVGDD IAWMKFDDEG RLRAINPERG FFGVAPGTSS
RTNPNAMATI ARNTIFTNVG LRSDGGVYWD GLDEPTEPGV TYTSWLGKPW KHGDPEPCAH
PNSRFCAPAD QCPIMDPRWD DPEGVPIDAI IFGGRRPRGV PLVVEAFGWR HGVFMGSAMR
SEATAAAEHK GGRLMHDPFA MRPFFGYNAG RYLEHWLSTG LRSNARLPRL FHVNWFLRDN
EGRFVWPGFG HNARVLAWIF GRIQGRDTAR PTPIGWVPKE GDLDLGGLPG VDYSQLFPME
KGFWEEECRQ LREYYGENFG ADLPRDVMAE LEGLEERVRK M
