ID J5JXL6_BEAB2 Unreviewed; 1368 AA.
AC J5JXL6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN ORFNames=BBA_04309 {ECO:0000313|EMBL:EJP67016.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP67016.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP67016.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP67016.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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}.
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DR EMBL; JH725158; EJP67016.1; -; Genomic_DNA.
DR RefSeq; XP_008597628.1; XM_008599406.1.
DR STRING; 655819.J5JXL6; -.
DR GeneID; 19887321; -.
DR HOGENOM; CLU_000395_1_1_1; -.
DR InParanoid; J5JXL6; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:EJP67016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..668
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 338..535
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 754..1022
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1292..1367
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 149963 MW; 2C35B55B97DE5250 CRC64;
MSDAASRKEA DHMDAATDSS NPLGGFPADG LFISTAWSED IWDRYIRDLN GKVAKHRAQW
YVVGAQFVCG VTVVGMTACG GIFTPPPPLP SPPPAYQRQL PSVFLAPEQP SSSSPSFFFL
PSHIFFPFNS RCFFATLLLC YKSPTMAPLP AASLPQQALT FNDVFEDVDD EPQQQHTVQH
IRANSSIMQL KKILGLYSQS PTVVKSLFEY AIILQNQTMV PNWPSFMLTP VSLRSRSSEL
YEDRLSMHRQ KADEAYVIGK RGQYTPVGAY LAGDEIIKIA VQHGAQLIHP ALPELTPLGY
GFLSENAEFA RNVEKAGLIF VGPSPDVIDA LGDKVSARKL AIAAQVPVVP GTEGAVATFE
EVKSFTDEYG FPIIIKAAYG GGGRGMRVVR DPDTLQESFE RATSEAKSAF GNGTVFVERF
LDKPKHIEVQ LLGDNHGNIV HLYERDCSVQ RRHQKVVEIA PAKDLPVETR DAILADAVKL
AKSVNYRNAG TAEFLVDQQN RYYFIEINPR IQVEHTITEE ITGIDIVAAQ IQIAAGATLA
QLGLTQDRIS TRGFAIQCRI TTEDPAKQFQ PDTGKIEVYR TAGGAGVRLD GGNGFAGSVI
TPFYDSMLVK CTCHGSTYEI ARRKVLRALI EFRVRGVKTN IPFLARLLTH PTFIDSNCWT
TFIDDTPELF DLLSSQNRGQ KLLAYLGDVA VNGSSIKGQI GEPKFKGEII IPEIVRSDGT
KVDVSEPCQK GWRNILVEQG PKAFAKAVRQ NKGCLLMDTT WRDAHQSLLA TRVRTVDLLN
IAKETSHALS NLFSLECWGG ATFDVAMRFL YEDPWDRLRK MRKLVPNIPF QMLLRGANGV
AYSSLPDNAI DQFVEQAKKN GVDIFRVFDA LNDIDQLEVG IKAVHKAGGV VEGTVCFSGD
MLNPKKKYNL EYYLDLVEKL VKLDIHILGI KDMAGVLKPH AATLLIGAVR EKYPDLPIHV
HTHDSAGTGV ASMVACAKAG ADAVDAATDS LSGMTSQPSI NAILASLEGT GLEPGLDPHQ
VRALDTYWSQ LRLLYSPFEA HLAGPDPEVY EHEIPGGQLT NMMFQASQLG LGSQWLETKK
AYEQANDLLG DIVKVTPTSK VVGDLAQFMV SNGLDAEAVK ARAGELDFPG SVLEFLEGMM
GQPYGGFPEP LRTDALRGRR KLDKRPGLYL EPVDFAQVKK DLGKKYGAPV TDCDIASHVM
YPKVFEDYRK FVAEYGDLSV LPTRFFLSKP EIGEEFNVEL EKGKVLILKL LAVGPLSENT
GQREVFFEMN GEVRQVTVID KTAAVENVSR LKADATDSSQ VGAPMSGVLV EMRVHEGSDV
KKGDPLAVLS AMKMEMVISA PHSGKVANLQ VKEGDSVDGS DLVCRITK
//