ID A0A077HJH5_9CORY Unreviewed; 1142 AA.
AC A0A077HJH5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=CUREI_02235 {ECO:0000313|EMBL:AIL96284.1};
OS Corynebacterium ureicelerivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL96284.1, ECO:0000313|Proteomes:UP000028939};
RN [1] {ECO:0000313|EMBL:AIL96284.1, ECO:0000313|Proteomes:UP000028939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL96284.1,
RC ECO:0000313|Proteomes:UP000028939};
RA Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT patient.";
RL Submitted (AUG-2014) 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 + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
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}.
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DR EMBL; CP009215; AIL96284.1; -; Genomic_DNA.
DR RefSeq; WP_038609923.1; NZ_CP009215.1.
DR AlphaFoldDB; A0A077HJH5; -.
DR STRING; 401472.CUREI_02235; -.
DR KEGG; cuv:CUREI_02235; -.
DR HOGENOM; CLU_000395_0_0_11; -.
DR OrthoDB; 9760256at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000028939; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 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 Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
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:AIL96284.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028939}.
FT DOMAIN 13..461
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 133..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 535..804
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1068..1142
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 487..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 616
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 714
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 743
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 745
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 878
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 714
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1108
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1142 AA; 124216 MW; 9DB0B05A80923D94 CRC64;
MNPDNLPLHD LPSFNKILVA NRGEIAVRAF RAAFETGAKT VAVYPREDRN SFHRPFADEA
VQIGEPGQPV KAYLDIDEII RAAKKTGADA VYPGYGFLSE RAELARACRD NGIKFIGPSP
ETLDLTGDKS AAVHAAERAG LPVLKDSEPS ADPKQLAEYA KEFEFPVFVK AVAGGGGRGM
RFIEKPEDVE RLAAEASREA EAAFGDPNVY IERAVINPQH IEVQIMADSY GNVVHLFERD
CSVQRRHQKV VEIAPAQHIT EEQRERICQD AVNFCKEINY EGAGTVEFLV DEAGNHVFIE
MNPRVQVEHT VTEEVTGIDI VKNQMYIAAG ASLEDVHLTQ DLIELNGAAL QCRITTEDPA
NGFRPDSGVV TGYQSPGGAG VRLDGNVAVG TTITPNFDSL LVKMTCRGRN FQVAVDRALR
ALNEFTINGL STNIGFLRAL LSEPEFRHER INTGFIADHP HLLEAPAAAD DAGKILNYLA
SVTVNQPNGP RPTNIRPSKK LPENTYGDLP RGSRDDLLEL GPAKWAEKLR NQTALGVTET
TFRDAHQSLL ATRVRTNTLV AAAKHVGHLT PQLTSVEAWG GATFDVGMRF LHESPWMRLD
EIREAMPNVN IQMLLRGRNT VGYTPYPDSV TKAFVQEAAT SGIDIFRIFD ALNDVSQMRP
AIDAVLETNT TVAEVAMAYS GNLLDPNEDL YTLDYYLNLA EQIVEAGAHV LAIKDMAGLM
RPAAAAKLVG ALRERFDLPV HVHTHDTAGG QLATYLAAAN AGADVVDVAS APLAGTTSQP
SMSALVAAFA NTERDTGIDL QSVFDMEPYW EAVRQVYAPF ESGIPGPTGR VYKHEIPGGQ
LSNLRTQAKA LGLEDRFELI EDYYAGVNEI LGRPTKVTPS SKVVGDLALQ LVGQGVSPEE
FAENPRKYDI PESVIGFLQG ELGTPPGGWP LLREKALENR SEVDHTVQVP DELAGDLASE
DHATRRAALD QLLFPKQYAE YQEHLRTYGI TDQLGDKAFF YGLEEGEETM IWYGEIDENR
PPLVVSLDAV SEPDEKGMRQ VILTVNGQVR PITVRDESAE SSVAEVEKAD SSNPGHVAAP
FAGAVTVTVK EGDEVKAGDP VATIEAMKME AAISATKDGK VERVAFTQPT KVEGGDLVVV
IA
//
