ID A0A166L4W8_9PEZI Unreviewed; 1596 AA.
AC A0A166L4W8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
DE Flags: Fragment;
GN ORFNames=CI238_10260 {ECO:0000313|EMBL:KZL63107.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL63107.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL63107.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL63107.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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}.
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:KZL63107.1}.
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DR EMBL; LFIW01002874; KZL63107.1; -; Genomic_DNA.
DR STRING; 1573173.A0A166L4W8; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 1.10.10.2790; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.472.90; Conserved carboxylase 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; IPR003604; Matrin/U1-like-C_Znf_C2H2.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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 SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF51569; Aldolase; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:KZL63107.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Zinc {ECO:0000256|ARBA:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 41..508
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 178..375
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1134..1249
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1519..1594
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL63107.1"
SQ SEQUENCE 1596 AA; 176840 MW; 154B20D805FD84C4 CRC64;
LPNMAQTAVT YNDVFEEGDV EEVQKDPQTI HHIRANSSIM HLKKILVANR GEIRKCFHST
ELLTQGKANR YPAIRAHELS LHTIAVFSYE DRLSMHRQKA DEAYVIGKRG QYTPVGAYLA
GDEIIKIAVE HGAQMVHPGY GFLSENAEFA RNVEKAGLIF VGPSADVIDS LGDKVSARKL
AIAADVPVVP GTEGAVATFE EVKGFTDQYG FPIIIKAAYG GGGRGMRVVR DQESLKESFE
RATSEAKSAF GNGTVFVERF LDKPKHIEVQ LLGDNHGNIV HLYERDCSVQ RRHQKVVEIA
PAKDLPSDVR DAILNDAVKL AKSVNYRNAG TAEFLVDQQN RYYFIEINPR IQVEHTITEE
ITGIDIVAAQ IQIAAGATLQ QLGLTQDRIS TRGFAIQCRI TTEDPSKGFQ PDTGKIEVYR
SAGGNGVRLD GGNGFAGAVI TPFYDSMLVK CTCHGSTYEI ARRKVLRALV EFRIRGVKTN
IPFLASLLTH PTFIDGNCWT TFIDDTPQLF DLIGSQNRAQ KLLAYLGDVA VNGSSIKGQI
GEPKFKGDII LPDLLNDDGS KLDVSQTCTK GWRQIIVEQG PKAFAKAVRD YKGTLLMDTT
WRDAHQSLLA TRVRTVDLLN IAKETSHGLH NLYSLECWGG ATFDVAYRFL YEDPWDRLRR
MRKAVPNIPF QMLLRGANGV AYSSLPDNAI DHFVEQAKKN GVDIFRVFDA LNDIDQLEVG
IKAVHKAGGV VEGTVCFSGD MLKSFAFFLE VSVFNFDLFV LSIARQHWLP RSVSLCNSSR
APLVEMETQP GTILEFVLWL SWTMLCLTPK SIKNSVFALL FPAKDDMEAI LLASGFQFAN
GLWDAIRSEV PPALSFFKGI PAEFSKRWAI YVLVLEKAGC RPKVYIGAGT EKRSGVSTRI
GQYRRGENFS TYVQKAVNEG FSIAHMGLLC WVPLPPASKR SSLRALVLVV EAAFTLWFWT
IRSRTSTYGM PSLGPWSPDS MEYDGCCGHF SLREGGAELM DRLSAEEIDA IDRERKLRNS
RRDALKRDKE GACLNAKKTR ANALSRKKWF CSFCNVNFGA RNQLRHHQTL QKHIDNVAGV
KRIVQNPRAK ERRAENFAAK RYYCELCDYT AKTQQKLNCH LATKKHPKKN PKKKYNLEYY
LNLVEKLVAL DIHVLGIKDM AGVLKPRAAE LLIGAIRKKY PDLPIHVHTH DSAGTGVASM
VACAKAGADA VDAATDSLSG MTSQPSINAI IASLEGSDHD TGLNPAHVRA LDSYWSQLRL
LYSPFEAHLS GPDPEVYEHE IPGGQLTNMM FQASQLGLGT QWAETKKAYE HANDLLGDIV
KVTPTSKVVG DLAQFMVSNK LTAEDVKARA GELDFPGSVL EFLEGLMGQP YGGFPEPLRS
NALRGRRKLD KRPGLFLEPV DFAKVKRELH KKFGGPVTEC DIAAYVMYPK VFEDYKKFIQ
KYGDLSVLPT KYFLSRPEIG EEFHVELEKG KVLILKLLAI GPLSENTGQR EVFYEMNGEV
RQVTVDDNKA SVENVSRAKA DPTDSSQVGA PMAGVLVELR VKEGSDVKKG DPIAVLSAMK
MEMVISAPHN GKVSTLQVKE GDSVDGSDLV CRIVKA
//
