GenomeNet

Database: UniProt
Entry: A0A1C3RHV5_9RHIZ
LinkDB: A0A1C3RHV5_9RHIZ
Original site: A0A1C3RHV5_9RHIZ 
ID   A0A1C3RHV5_9RHIZ        Unreviewed;      1149 AA.
AC   A0A1C3RHV5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-JUN-2019, entry version 16.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   Name=pyc {ECO:0000313|EMBL:SCA56845.1};
GN   ORFNames=MTBPR1_30215 {ECO:0000313|EMBL:SCA56845.1};
OS   Candidatus Terasakiella magnetica.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylocystaceae; Terasakiella.
OX   NCBI_TaxID=1867952 {ECO:0000313|EMBL:SCA56845.1, ECO:0000313|Proteomes:UP000231658};
RN   [1] {ECO:0000313|Proteomes:UP000231658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lefevre C.T.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step
CC       and the transfer of the carboxyl group to pyruvate in the second.
CC       {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=6.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
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DR   EMBL; FLYE01000023; SCA56845.1; -; Genomic_DNA.
DR   RefSeq; WP_069188908.1; NZ_FLYE01000023.1.
DR   Proteomes; UP000231658; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 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   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   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 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; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Complete proteome {ECO:0000313|Proteomes:UP000231658};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:SCA56845.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:SCA56845.1}.
FT   DOMAIN        7    461       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      127    325       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      537    805       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1074   1149       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   REGION     1063   1083       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1C3RHV5}.
FT   ACT_SITE    300    300       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       546    546       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       715    715       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       744    744       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       746    746       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     123    123       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     207    207       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     618    618       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     879    879       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1149 AA;  125778 MW;  6E8356DC0D621DD7 CRC64;
     MINRPEKIRR LLAANRGEIA IRICRAASEL GIETVAIYSN EDRFALHRFK ADESYLIGEG
     KGPVEAYLDI ETIIRVAKDA NVDAIHPGYG LLSENPTFAR RCEEEGLIFV GPKAEVMEGL
     GNKVSARNLA VRAGAPVVPA TNALPDDEEV IKAEAAKVGY PMITKASWGG GGRGMREIES
     EAELLQQVDA AKREAKAAFG NDELYLEKLV RRARHVEVQI IGDTHGNVVH LFERDCSVQR
     RNQKVVERAP APYLNDEKRT ELCEAALKIA RTANYSCAGT VEFLMDVDTE EFYFIEVNPR
     VQVEHTVTEV VTGIDIVQAQ IRICEGAMIG RDDSGVPAQE DIKLNGHSIQ CRVTTEDPEN
     NFIPDYGKIL AYRGATGFGI RLDGGTAFSG ALVTRYYDSL LEKVTAWGAS PNEAVARMDR
     ALREFRIRGV ATNLTFLENV LSHEKFLTGA YTTKFIDTAP ELFDMPKRQD RASKLLNFLG
     EVMVNGNPEV AGRIHPNHIH HPSAPNYAVP IGDGLKQKLA NEGPKAVADW MLAQDRLLLT
     DTTMRDAHQS LLATRVRTDD LVKIAPSYAA RLPELFSVEC WGGATFDVAM RFLKECPWER
     LERLSAAMPN HLTQMLLRAS NGVGYTNYPD NAVKYLVERA ANAGMDVFRV FDSLNWVENM
     RVAMDAVLDT GKMCEATVCY TGDTLDANRS KYDLKYYVDM AKELEGAGAH ILAIKDMAGL
     LKPAAATQLF SALKNEISIP VHFHTHDTSG IAAASILAAA EAGVDAVDAA LDSMSGLTSQ
     ANLGSIVAAL KNTPRDTGLD QTALRKVSDY WEAVRANYVG FESDIRCGTS DVYNHEMPGG
     QYTNLRQQAR SLGIEEHWSE VSDAYADVNQ MFGDIVKVTP SSKVVGDMAL MMVTSSLSRD
     DVENPDKEIA FPDSVVSFFK GELGQPTGGF PKALQDKVLK GETPITVRPG SVMDPLDLDA
     ERKAAEEIAG RTISENELAS YIMYPAVFRD YVSHQNEFGD VTVLPTGAFF YGMEAGEEMA
     VDIAKGKTLF IRFRAMSDAD EEGRRTVFFE LNGQPRNVKI TDKATAPQKE AAPKAEDGNE
     NHVGAPMPGL VVSVAVKEGD EVERGDVLCS IEAMKMETSV LAEKSGTIER VVSSAGTQVD
     TKDLLVVLG
//
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