ID A0A318AI25_9MICC Unreviewed; 1171 AA.
AC A0A318AI25;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=DCC25_01980 {ECO:0000313|EMBL:PXA81354.1};
OS Auritidibacter sp. NML120636.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Auritidibacter.
OX NCBI_TaxID=2170743 {ECO:0000313|EMBL:PXA81354.1, ECO:0000313|Proteomes:UP000247286};
RN [1] {ECO:0000313|EMBL:PXA81354.1, ECO:0000313|Proteomes:UP000247286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML120636 {ECO:0000313|EMBL:PXA81354.1,
RC ECO:0000313|Proteomes:UP000247286};
RA Bernard K., Pacheco A.L., Burdz T., Wiebe D., Beniac D., Booth T.,
RA Goldenberger D., Seth-Smith H., Egli A., Bernier A.-M.;
RT "Auritidibacter winnipegensis sp. nov. recovered from Human Clinical
RT Materials and Emendation of the Genus Auritidibacter (Yassin et al 2011).";
RL Submitted (MAY-2018) 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 -!- 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:PXA81354.1}.
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DR EMBL; QHLO01000002; PXA81354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318AI25; -.
DR Proteomes; UP000247286; Unassembled WGS sequence.
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:InterPro.
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; 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; 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|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:PXA81354.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247286}.
FT DOMAIN 20..473
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 140..340
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 564..833
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1094..1168
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 573
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 645
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 743
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 772
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 774
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 907
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 743
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1134
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1171 AA; 127448 MW; 61CF19FF26237791 CRC64;
MASKDSVQPN RPAQSDQPTG FSKVLVANRG EIAVRAFRAC YELGAKTVGV FPYEDRNSIH
RQKADEAYLI GEEGHPVRAY LDVDEIIRVA QQADAEAIYP GYGFLSENPE LARKTAEAGL
TFVGPPAGVL EVTGNKVASL RAARQAGIPT LQSTDPTDDA EALIAQADDI GYPLFVKAVA
GGGGRGMRRV EHAKDLPDAL SAAMREADTA FGDPTVFLEQ AVVRPRHIEV QVLADSQGNV
VHIFERDCSM QRRHQKVVEM APAPNLDDSI RQALYRDAVK FAKSMNYVNA GTVEFLVDTA
GERAGEHFFI EMNPRIQVEH TVTEEVTDID LVSSQLRIAT GESLEDLGIT QENLRLRGAA
IQCRITTEDP ANDFRPDTGT VSAYRSAGGS GIRLDGGTIY TGAEISPHFD SMLVKLTGRG
RDFAAARRRV RRALAEFRIR GVATNIPFLL NVLDDPQFIA GDVATDFIDQ HPELTQINRS
KNRGSRALQY LADVTVNQPH GPRVEGIDPR DKLPSFPGDK REEPERSPFD GVSHKVEPPA
GWRKVLLHKG PEGFATALRE HQGLAVTDTT FRDAHQSLLA TRIRTRDLLA AAPAVSHRLS
QLFSAEIWGG ATYDVALRFL AEDPWDRLAR LREAMPNIPL QMLLRGRNTV GYTPYPQEVT
EAFVAEAAET GIDIFRIFDA LNDVEQIIPA ITAVRERTSA VAEAALCYTG NLLDPDEKLY
TLDYYLNLAE RMVDAGAHVL GIKDMAGLLR PEAARRLVTE LRSRFDVPVH LHTHDTAGGQ
LATLLAASEA GVDAVDVAVA SMSGTTSQVS MSALVAATNF TDRETGLGLD DVASLEPYWE
TVRSIYAPFE SGIPASTGRV YQHEIPGGQL SNLRQQAISL GLADRFEQIE DMYGAANKIL
GNLVKVTPSS KVVGDLALAL VSAQADPADF EENPQNYDIP SSVIDFLSGQ LGDPPGGWPE
PFRAKALQGR ETSPQQDETV SAEDSAALKR SGRERQETLN RLLFPGPTRE YEEHTRRYGD
TSVLHTRDFL YGMTKGMEHV ISLGTGVRLL ATLQSISEPD EKGMRTVMVT LNGQARQLEV
RDNSVESTVR SAEKADRDQP GHIAAPFAGA VTVQVEEGDT VDAGDTVATI EAMKMEAAIT
TQVAGTVKRV VLTEPTPVDG GDLVLVIDPE N
//
