GenomeNet

Database: UniProt
Entry: E6U459_ETHHY
LinkDB: E6U459_ETHHY
Original site: E6U459_ETHHY 
ID   E6U459_ETHHY            Unreviewed;      1140 AA.
AC   E6U459;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN   OrderedLocusNames=Ethha_1006 {ECO:0000313|EMBL:ADU26559.1};
OS   Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 /
OS   YUAN-3).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ethanoligenens.
OX   NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU26559.1, ECO:0000313|Proteomes:UP000001551};
RN   [1] {ECO:0000313|EMBL:ADU26559.1, ECO:0000313|Proteomes:UP000001551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3
RC   {ECO:0000313|Proteomes:UP000001551};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A.,
RA   Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.;
RT   "Complete sequence of Ethanoligenens harbinense YUAN-3.";
RL   Submitted (DEC-2010) 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 and
CC       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(+) + 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|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953,
CC         ECO:0000256|PIRNR:PIRNR001594};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002400; ADU26559.1; -; Genomic_DNA.
DR   RefSeq; WP_013484920.1; NZ_CP025286.1.
DR   AlphaFoldDB; E6U459; -.
DR   STRING; 663278.Ethha_1006; -.
DR   KEGG; eha:Ethha_1006; -.
DR   eggNOG; COG1038; Bacteria.
DR   HOGENOM; CLU_000395_0_1_9; -.
DR   OMA; YAIQSRV; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001551; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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: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   PIRSF; PIRSF001594; Pyruv_carbox; 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|PIRNR:PIRNR001594};
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:ADU26559.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001551}.
FT   DOMAIN          4..457
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          124..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          529..797
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1064..1139
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         538
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         610
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         707
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         736
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         738
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         871
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         707
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1105
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1140 AA;  126893 MW;  61AF399CE9F1DD94 CRC64;
     MQRKIEKVLV ANRGEIAIRI FRACYDMSLR TVAIYSKEDV FNLFRTKADE AYMLDENKSP
     LAAYLDINYI IDLAKRKGVD AVHPGYGFLS ENADFARACE ENGIIFIGPP SDVLEKMGSK
     LNAKAIANSC NVPVIPGSTD QIKDLDDALE RADSYGYPVL LKAAAGGGGR GMRRVDSPEE
     MGIALDLVRG EAKKAFGDDS IFMEKFLVNP KHIEVQILAD EQGNTVHLFE RDCSLQRRYQ
     KVVEFAPAFS IPEATRRKLY DDAVKIAKCV HYVNAGTVEF LVDQNGNHYF IEMNPRIQVE
     HTVTEMITGI DLVRAQILIA QGLPLSAPGI DIQSQDSVKK SGFAIQSRVT TEDPRNNFAP
     DCGKITTYRS GGGFGVRLDA GNAYAGAEVS PYYDSLLVKI TTYDRTFENT IRKALRAITE
     IHIHGVKTNM AFLCNILAHP AFQAGVCHTK FIDETPELFE FEDPRNRATK ILKYIGDLIV
     NEKEKPKIPL EKPRIPSAPN AEPPKGLKQL LDSEGPAGFQ KYVLEQKKLL LCDTTMRDAH
     QSLLATRVRT KDLVSIAEPT AHLLPDLYSV EMWGGATFDV AYRFLHESPW DRLSQLRALI
     PNIPFQMLLR GANAVGYTNY PDNLIRAFIR EAAAGGIDIF RIFDSLNWIP GMEVALDEVI
     KCGKVAEATI CYTGDILDPH QTKYTLQYYV DMAKELERRG AHILCIKDMS GVLKPYAAKQ
     LVTALKQEIG IPVHLHTHDT SGNQMAALLL AAETGVDVVD TAIASMSSLI SHPSLNSIVA
     ALQGQERDTG IDPYSLTPLT DYWADVRKTY YQFEANRNYP DVEIYKYQIP GGQLTNLKRQ
     IESLGLGHRF EEVKEKYKEA NSILGDIVKV TPSSKVVGDL AIFMTQNDLT AENIVERGKR
     LTFPDSVVSY FKGMIGQPAW GFPEDLQEVV LKGEKPITCR PGELLEPIDF EQVKAKITKY
     EKNPSMQDLV SWCLYPKVLE DYCKRRQEYG DISRMDSHVF FLGMEQGEMT ELSIEEGKTL
     IIKYVGLGEM NSDGTQNVVF ELNGARREVA VRNDAKVAES SVLMADMDDN TQIGASIPGA
     VSKVLVKSGE EVKKNQVLAI IEAMKMETSI VSNIDGLIDK VFITEGKSVE AGELLFTVKE
//
DBGET integrated database retrieval system