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Database: UniProt
Entry: J5JXL6_BEAB2
LinkDB: J5JXL6_BEAB2
Original site: J5JXL6_BEAB2 
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
//
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