ID A0A0G4MA57_9PEZI Unreviewed; 1546 AA.
AC A0A0G4MA57;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN ORFNames=BN1708_005367 {ECO:0000313|EMBL:CRK31177.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK31177.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK31177.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK31177.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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}.
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DR EMBL; CVQH01021640; CRK31177.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4MA57; -.
DR OrthoDB; 1129179at2759; -.
DR Proteomes; UP000044602; 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-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; 2.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 3.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
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; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00289; Biotin_carb_N; 2.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF00682; HMGL-like; 2.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 3.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS50979; BC; 2.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 2.
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:UP000044602}.
FT DOMAIN 36..261
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 158..213
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 264..1546
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 386..583
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 684..1064
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1255..1527
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1469..1544
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1546 AA; 168899 MW; 68593844FCEA1739 CRC64;
MAQTAVTFSD VFDDSDGDAP KGQSIHHIRA NSSIMQLKKI LVANRGEIPI RIFRTAHELS
LHTIAVFSYE DRLSMHRQKA DEAYVIGKRG QYTPVGAYLA GDEIIKIAVE HGAQMIHPGY
GFLSENAGFA RNVEKAGLIF VGPSPDVIDS LGDKVSARKL AIAADVPVVP GTEGAVATFE
EVKTFTDQYG FPIIIKAAYG GGGRGMRVVR EQESLKESFE RATSGALEMA QTAVTFSDVF
DDSDGDVPKG QSIHHIRANS SIMQLKKILV ANRGEIPIRI FRTAHELSLH TIAVFSYEDR
LSMHRQKADE AYVIGKRGQY TPVGAYLAGD EIIKIAVEHG AQMIHPGYGF LSENAGFARN
VEKAGLIFVG PSPDVIDSLG DKVSARKLAI AADVPVVPGT EGAVATFEEV RTFTDQYGFP
IIIKAAYGGG GRGMRVVREQ ESLKESFERA TSEAKSAFGN GTVFVERFLD KPKHIEVQLL
GDNHGNIVHL YERDCSVQRR HQKVVEIAPA KDLPVETRDA ILADAVKLAR SVNYRNAGTA
EFLVDQQNRY YFIEINPRIQ VEHTITEEIT GIDIVAAQIQ IAAGATLDQL GLTQDRISTR
GFAIHQNRAQ KLLSYLGDIA VNGSRIKGQV GEPKFKGDII QPILLNPDGS RLDTSAPATK
GWRQILLDQG PKAFAKAVRD YKGCLLMDTT WRDAHQSLLA TRVRTVDLLN IAHETSHALS
NLYSLECWGG ATFDVAMRFL YEDPWDRLRR MRKLVPNIPF QMLLRGANGV AYSSLPDNAI
EQFVDQAKKC GVDIFRVFDA LNDVSQIEVG VKAVHKAGGV VEAVACYSGD MLVCTFFLFV
IAFFFHRVGP PLGSECLLSY SSYSQAAVPG IWSSSSVLPF TPISFPLSPL PLIFITTQAI
SRLVFNTPEC LSFVVLPHCP SPQVFVQFLC SKLLNRKLRN PRRDNPNKKY NLQYYLDLVD
KLVALDIHVL GIKDMAGVLK PHAATLLIGA IREKYPDLPI HVHTHDSAGT GVASMVACAK
AGADAVDAAT DSLSGMTSQP SINAILASLE GSDLDPGLNP AHVRALDTYW SQLRLLYSPF
EAHIAGPDPE VYEHEIPGGQ LTNMMFQAQQ LGLGTQWAET KKAYEHANDL LGDIVKVTPT
SKVVGDLAQF MVSNKLSPED VKARAGELDF PGSVLEFLEG MMGQPYLGDV AVNGSRIKGQ
VGEPKFKGDI IQPILLNPDG SKLDTSAPAT KGWRQILLDQ GPKAFAKAVR EYKGCLLMDT
TWRDAHQSLL ATRVRTVDLL NIAHETSHAL SNLYSLECWG GATFDVAMRF LYEDPWDRLR
RMRKLVPNIP FQMLLRGANG VAYSSLPDNA IEQFVDQAKK CGVDIFRVFD ALNDVSQIEV
GVKAVHKAGG VVEAVACYSG DMLVCTNPNK KYNLQYYLDL VDKLVALDIH VLGIKDMAGV
LKPHAATLLV RQVTVDDNKA SVENVTRPKA DLSDSSQVGA PMAGVLVELR VKEGSDVKKG
DPIAVLSAMK MEMVISAPHN GQVSSLQVKE GDSVDGSDLV CKIVKA
//
