ID Q16921_AEDAE Unreviewed; 1195 AA.
AC Q16921;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 136.
DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN Name=5572254 {ECO:0000313|EnsemblMetazoa:AAEL009691-PB};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:AAB64306.1};
RN [1] {ECO:0000313|EMBL:AAB64306.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9066123; DOI=10.1016/S0965-1748(96)00078-1;
RA Tu Z., Hagedorn H.H.;
RT "Biochemical, molecular, and phylogenetic analysis of pyruvate carboxylase
RT in the yellow fever mosquito, Aedes aegypti.";
RL Insect Biochem. Mol. Biol. 27:133-147(1997).
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL009691-PB, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL009691-PB,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AAEL009691-PB}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL009691-PB};
RG EnsemblMetazoa;
RL Submitted (OCT-2022) to UniProtKB.
CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC carboxylation of the covalently attached biotin in the first step and
CC the transfer of the carboxyl group to pyruvate in the second.
CC {ECO:0000256|PIRNR:PIRNR001594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953,
CC ECO:0000256|PIRNR:PIRNR001594};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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DR EMBL; L36530; AAB64306.1; -; mRNA.
DR PIR; T43735; T43735.
DR AlphaFoldDB; Q16921; -.
DR EnsemblMetazoa; AAEL009691-RB; AAEL009691-PB; AAEL009691.
DR EnsemblMetazoa; AAEL009691-RC; AAEL009691-PC; AAEL009691.
DR VEuPathDB; VectorBase:AAEL009691; -.
DR HOGENOM; CLU_000395_0_1_1; -.
DR InParanoid; Q16921; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01235; pyruv_carbox; 1.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:AAB64306.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820}.
FT DOMAIN 37..487
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 157..354
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 580..849
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1120..1195
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 329
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 589
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 661
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 758
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 788
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 790
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 925
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 758
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1161
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1195 AA; 132202 MW; D4F583138D49BFC1 CRC64;
MSMCGAQIAL KAFKRAPRVR IWSMTKNAYS TKIEYKPIRS VLVANRGEIA IRVFRACNEL
GIRSVAVYSE QDKMHMHRQK ADESYMVGKG LAPVEAYLSI PEIIRVCKEN DVDAVHPGYG
FLSERSDFAQ AVIDAGLRFI GPSPKVVQQM GDKVAARKAA IEAGVPIVPG TDGPVTTKEE
ALDFCKKHGL PVIFKAAYGG GGRGMRVVRK MEEVEDNFQR ASSEAKAAFG NGAMFIEKFI
ERPRHIEVQL LGDKAGNVVH LYERDCSVQR RHQKVVEIAP APRLPREVRD KMTEYAVKLA
KHVGYENAGT VEFLCDESGN FYFIEVNARL QVEHTVTEEI TGIDLVQSQI RVAEGMTLPE
LGYNQENIKT QGYAIQCRVT TEDPANDFQP STGRLEVFRS GEGMGIRLDS ASAYAGAIIS
PYYDSLLVKV ISHASDLQSS AAKMNRALRE FRIRGVKTNI PFLLNVLENQ KFLNGVLDTY
FIDEHPQLFR FAKSKNRAQK LLNYLGEVLV NGPTTPLATK LKPAEVQPHV PQLPLDLSPE
ALAAEEKGKK VTEPPRGFKD ILREQGPEGF AKAVRAQKNL LLMDTTFRDA HQSLLATRVR
THDLLKISPY VSHKFNNLYS LENWGGATFD VALRFLHECP WERLEDMRKQ IPNIPFQMLL
RGANAVGYTN YPDNVVHKFC ELSVQCGMDI FRVFDSLNYL PNLILGMEAA GNAGGVVEAA
ISYTGDVSDP TKKKYDLKYY TNLADELVKA GTHILCIKDM AGLLKPQAAK LLIAAIREKH
PDVPIHIHTH DTSGAGVASM LACAEAGADV VDVAVDSMSG MTSQPSMGAV VASLQGTPLD
TGLNLRDISE YSAYWEQTRT LYAPFECTTT MKSGNADVYL NEIPGGQYTN LQFQAYSLGL
GDFFEDVKKA YREANLLLGD IIKVTPSSKV VGDLAQFMVQ NHLTADQVME RAEELSFPKS
VIEFLQGAIG TPHGGFPEPF RSRVLKDMPR IEGRPGASLN PLDFDKLKKD LQESHPDVSD
RDVMSAALYP QVTNDYLNFR DSFGPVDKLD TRVFLTGPKV GEEFEVTIEK GKTLGFKTLA
MAEDLTSNGE REVFFELNGQ LRSVMVRDKE AVKELHIHPK ATKGNKDQVG APMPGSVIEI
KVKVGDRVEK GQPLVVLSAM KMEMVVQSPR AGVVKSLDIS SGMKLEGEDL ILTLE
//
