ID A0A1Y2BE15_9TREE Unreviewed; 1227 AA.
AC A0A1Y2BE15;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN ORFNames=BCR39DRAFT_330344 {ECO:0000313|EMBL:ORY33078.1};
OS Naematelia encephala.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Naemateliaceae; Naematelia.
OX NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY33078.1, ECO:0000313|Proteomes:UP000193986};
RN [1] {ECO:0000313|EMBL:ORY33078.1, ECO:0000313|Proteomes:UP000193986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-887.2 {ECO:0000313|EMBL:ORY33078.1,
RC ECO:0000313|Proteomes:UP000193986};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:ORY33078.1}.
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DR EMBL; MCFC01000007; ORY33078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2BE15; -.
DR STRING; 71784.A0A1Y2BE15; -.
DR InParanoid; A0A1Y2BE15; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000193986; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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 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|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000193986}.
FT DOMAIN 72..522
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 192..389
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 610..879
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1145..1223
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 45..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 134112 MW; A4D9151AFF8C8100 CRC64;
MANVFVSRPP SPNPIDITSY THVPPSTHSQ IEAWVSHLGI DTSLPSTPSS PSLSNNPTIH
NLRRKQAGHS GPLKKVLVAN RGEIAIRVFR TAHELAMSTV AIYSYEDRMG AHRYKSDESY
LVGKGLTPVG AYLAQDDIIR LALEHEVDMI HPGYGFLSEN AEFAKKVEDA GIAFIGPRPE
TIDALGDKTK ARTLAMKTDV PVVPGTPGPV ESYDKASAFI EQYGFPVIIK AAMGGGGRGM
RVVRDQESFK ENFERAVSEA KSAFGDGTVF IERFLDHPRH IEVQLLADGE GNCVHLFERD
CSVQRRHQKV VEIAPAPHLD ESIRQAILSD ALKLAAAVKY RNAGTAEFLV DQQGRHYFIE
INPRIQVEHT ITEEITGIDI VAAQIQIAAG VTLEQLGLTQ EHIHRRGFAI QCRITTEDAA
AGFQPDTGKI EVYRSAGGNG VRLDASSGYA GAQITPHYDS LLVKCSVSGA TFEVARRKML
RALVEFRIRG VKTNIPFLIR LLTHPVFESG KTWTTFIDDT PDLFKLVHSQ NRAQKLLAYL
GDISVNGSSI AGQMGEPGLK TAAIIPQIRD VNDSSKIIDT SESCTTGWRN IIVKEGPEAF
AKAIRAYKGC LIMDTTWRDA HQSLLATRMR TVDMANIAKE TSHALQNAYS LECWGGATFD
VAMRFLYEDP WDRLRTLRKL VPNIPLQALV RGANAVGYTS YPDNAIYEFS KKAVEAGLDI
FRVFDSLNYF ENLKLGIDAA KKAGGVVEGT ICYSGDVANP KRTKYTLQYY LDLTDQLVGE
GIHVLGIKDM AGLLKPEAAK ILIGAIRKAH PDLPIHVHSH DTAGIAAASM LACALAGADV
VDVAIDDLSG LTSQPAMGAV CSALEQTGLG TGISHENIQA LNMYWSQIRV LYGCFEANVR
ASDSGVFDHE MPGGQYTNLQ FQASQLGLGT QWLEIKKKYI EANQLCGDII KVTPSSKVVG
DFAQFMVSNQ LSKQDVIDKA ATLDFPSSVV EFFQGFLGQP YGGFPEPLRS NIIRDKPRID
GRPGIGMKPL DFKKIKAELR EKFGQHITDY DVASYCMYPK VFEEFQGFVE KYGDLSVVPT
RYFLAKPEIG EELTISIEKG KTLTIKLLAV GPLNTEKGTR ECFFELNGES RAVVITDRNA
AIEHVAREKA TSDPGSVGSP MGGVVIDVRV KEGQDVKAGD PLCVLSAMKM ESVVSSPVSG
KVKRVLVRES DSIGQGDLVV EITHGTK
//
