ID C5PE04_COCP7 Unreviewed; 1196 AA.
AC C5PE04;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
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 ORFNames=CPC735_019190 {ECO:0000313|EMBL:EER25315.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER25315.1, ECO:0000313|Proteomes:UP000009084};
RN [1] {ECO:0000313|EMBL:EER25315.1, ECO:0000313|Proteomes:UP000009084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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 -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC the ATP-dependent carboxylation of the covalently attached biotin in
CC the first step and the transfer of the carboxyl group to pyruvate in
CC the second. {ECO:0000256|ARBA:ARBA00002380}.
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|ARBA:ARBA00000564,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EER25315.1}.
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DR EMBL; ACFW01000043; EER25315.1; -; Genomic_DNA.
DR RefSeq; XP_003067460.1; XM_003067414.1.
DR AlphaFoldDB; C5PE04; -.
DR GeneID; 9692931; -.
DR KEGG; cpw:CPC735_019190; -.
DR VEuPathDB; FungiDB:CPC735_019190; -.
DR HOGENOM; CLU_000395_0_1_1; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
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; 1.
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; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
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}; Pyruvate {ECO:0000313|EMBL:EER25315.1}.
FT DOMAIN 44..496
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 166..363
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 582..850
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1119..1194
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 338
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 591
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 663
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 759
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 789
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 791
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 924
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 759
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1160
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1196 AA; 131029 MW; 34B4E6A8849BAFFC CRC64;
MAASNPAVSV VPEEAIDDVV EDHSPSNYEH SVHRRLRANS TIMQFHKILV ANRGEIPIRI
FRTAHELSLQ TVAVYSYEDR LSMHRQKADE AYMIGRRGQF TPVGAYLAGD EIIRIAVQHG
VHLIHPGYGF LSENAEFARN VEKAGLVFVG PTPDTIDALG DKVSARRLAI KCGVPVVPGT
EGPVSRFEEV KAFTDQYGFP IIIKAAFGGG GRGMRVVRDQ ESLRDSFERA TSEAKSAFGN
GTVFVERFLD RPKHIEVQLL GDNHGNVVHL YERDCSVQRR HQKVVELAPA KDLPVDVRDS
ILADAVKLAK SVSYRNAGTA EFLVDQLNRY YFIEINPRIQ VEHTITEEIT GIDIVAAQIQ
IAAGATLEQL GLTQDRISTR GFAIQCRITT EDPTKGFQPD TGKIEVYRSA GGNGVRLDGG
NGFAGSIITP HYDSMLVKCT CHGSTYEIVR RKMLRALVEF RIRGVKTNIP FLASLLTHPT
FIQGTCWTTF IDDTPELFAL IGSQNRAQKL LAYLGDVAVN GSRIKGQIGE PKFKGAISMP
TIVDEAGTPV DVSVPCQKGW KQILDEQGPA AFAKAVRANK GCLIMDTTWR DAHQSLLATR
VRTVDLVNIA KETSHAYSNA YSLECWGGAT FDVAMRFLYE DPWDRLRKLR KAVPNIPFQM
LLRGANGVAY SSLPDNAIYH FCKQAKKYGV DIFRVFDALN DIHQLEVGMK AVQAAGGVVE
GTLCYSGDML NPNKKYNLNY YLDLVDKIVA LGTHVLGIKD MAGVLKPQAA TMLIGAIRKK
YPDLPIHVHT HDSAGTGVAS MVACALAGAD AVDAATDSMS GMTSQPSVGA ILASLEGTEC
DPKLDIRNIR AIDSYWAQLR LLYSPFEAGL TGPDPEVYEH EIPGGQLTNL IFQAHQLGLG
TQWAETKKAY KQANDLLGDI VKVTPTSKVV GDLAQFMVSN KLTPDDVIAR AGELDFPGSV
LEFLEGLMGQ PYGGFPEPLR SKALRDRRKL DSRPGLHLPP LDLVKIKADL KEKYGTATEC
DVASFAMYPK VYEDYRNFVS KYGDLSVLPT KYFLSRPEIG EEFSVELEQG KVLILKLLAV
GPLSEQTGQR EVFYEMNGEV RQVAVDDILA AVDNTSRPKA DPNNSSQVGA PMSGVVVEIR
VHDGLEVKKG DPIAVLSAMK MEMVISAPHH GTISGLLVKE GDSVDGQDLI CTIHKV
//