ID C4JI85_UNCRE Unreviewed; 1131 AA.
AC C4JI85;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=UREG_02831 {ECO:0000313|EMBL:EEP77982.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP77982.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
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};
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DR EMBL; CH476615; EEP77982.1; -; Genomic_DNA.
DR RefSeq; XP_002543315.1; XM_002543269.1.
DR AlphaFoldDB; C4JI85; -.
DR STRING; 336963.C4JI85; -.
DR GeneID; 8437620; -.
DR KEGG; ure:UREG_02831; -.
DR VEuPathDB; FungiDB:UREG_02831; -.
DR eggNOG; KOG0369; Eukaryota.
DR HOGENOM; CLU_000395_1_0_1; -.
DR InParanoid; C4JI85; -.
DR OMA; MHTHDTN; -.
DR OrthoDB; 1129179at2759; -.
DR Proteomes; UP000002058; 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-KW.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
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 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; 2.
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; 2.
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; PS00866; CPSASE_1; 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 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:EEP77982.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT DOMAIN 2..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 143..346
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 522..780
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 555
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 689
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 719
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 721
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 854
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 689
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1092
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1131 AA; 124168 MW; 526BE636A84330A7 CRC64;
MKQLKVLVAN RGEIASRILV AAHELGMATV ALYSEEDRFA GYRKGLFGMD SIVASYEKLT
GFAEADESYL VGNQPDIGPV QAYLDGANII EIAKQHRVDL IHPGYGFLSE NADFAAQVRA
AGLKFVGPRT ETIREMGDKV TARRIAQRFG VPTIPGTNGP VRNLQDAYDF VETHGFPVII
KASFGGGGRG MRVVHQKGAL EEAISAARSE ANAAFGDGAI FMEKFLDRPK HIEVQILSDY
HGNHVHICER DCSVQRKHQK VVEFAPAVSI SQHVRWGVLD AAVTLAQGLD YGKNSFSYAF
VAQVEHTVTE EVTGIDIVAA QLRIACGTSL KELGLTQQKI ETRGFAIQCR VTTEIPSEGF
RPDNGTISGC RLPTGNGVRL DHSECFLGAR ISPFYDSLLV KCICSGPDFA SVISRTIRAL
KQFQIRGIQT NLEFLIQLLK HPTFAAGNCW TSFVDDTPEL FHLNGQIDPA QGLMRFLGDA
AVNGSRVQGQ TKPPGLKRDI TIGKLTGPKS GDEINTDIPC QQGWRNILTR YGPQAFAQQV
RAHRKTLITD TTWRDGQQSL LATRVRSKDL DAIAKHVSYA YQAAYSLECW GGATFDVMLR
FLLPDNALFH FVKLAKDTGV DIFRVFDSLN DLENLKVGIE AVHAAGGLVE GAVMYTGDML
EPGNKYNLEY YLGIVDRLVE YGSHVIAIKS MSGVMKPAAG RALVKAIRLR YPDIPIHMHT
HDTNGTGTAT MLACVEEGAD IVDTAIDSLS GSTSQPAVGA VVASLQNTEF ESALHLDQIR
MIDAYWAQLR LVYAGFDADL RSPDPTVYKH EIPGGQYSNL IFQARENGLG DKWDKTLKAY
EDANQLLGDI IKATPTSKAV GDLAQLMVDL KISAAEVQER ASKLDFPQSV VDYFEGLMGQ
PLGGFPEPLR TRILRGSPAS IKQRPGLTMK PIDFNHVRQE ISSRFPGSSV TEYDVASYVM
YPEVYMGFRQ ARQEFGDLTT LRTPDFLLPP EIGQEVQLKL DDGQEVVAEM LAIRPADPVT
GKREVLFRLN GEVCFVTVQD DKATPKRKLR KANPKVEREL AAPVAGRIAR LMVVSGDTVK
AGETLLTVSA MKMRYGSMCY EARGILSSSH KSSNKGSRLF LINLLDNTVQ R
//
