ID A0A327QS94_9BACT Unreviewed; 1148 AA.
AC A0A327QS94;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=LX64_01892 {ECO:0000313|EMBL:RAJ06765.1};
OS Chitinophaga skermanii.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=331697 {ECO:0000313|EMBL:RAJ06765.1, ECO:0000313|Proteomes:UP000249547};
RN [1] {ECO:0000313|EMBL:RAJ06765.1, ECO:0000313|Proteomes:UP000249547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23857 {ECO:0000313|EMBL:RAJ06765.1,
RC ECO:0000313|Proteomes:UP000249547};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-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 -!- 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:RAJ06765.1}.
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DR EMBL; QLLL01000003; RAJ06765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327QS94; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000249547; 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: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 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:RAJ06765.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249547}.
FT DOMAIN 8..461
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 539..806
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1072..1148
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 548
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 620
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 716
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
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 747
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 880
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 716
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1114
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1148 AA; 128442 MW; A25E8E2DA23F7E0F CRC64;
MSDTSLKKIQ KLLVANRGEI AVRILRAAAE LRIRTVAIFT YEDRYSLHRY KADEAYQVGK
NDDPLKPYLD IEGIIHLAKE QGVDAIHPGY GFLSENVQFA KRCKEEGIIF VGPDVEVMAQ
LGDKVAAKKL AREVKVPLIE DSEAKLIDTA TALSEAKRIG FPIILKAAAG GGGRGMRVVR
EESQLEKSFT EARSEAGKAF GDDTIFIEKF IEEPKHIEVQ LMGDNYGNIV HLYERDCSVQ
RRFQKVVEIA PSPNLPLETR EEIYGYALAL AKKVNYNNVG TVEFLVDRSN KVYFIEVNPR
IQVEHTVTEE VTGIDIVRSQ ILIAQGHQLS DPEIFLKSQD DVKLNGFAIQ CRITTEDPEN
GFKPDYGTVI AYRNAGGFGI RLDEGSTYSG VKISPFFDSM LVKVTAWGRT LSGSSARLHR
TLREFRIRGV KTNISFLENV ITHDIFRKGN CTVSFIDQNP ELFKLSPIRD RATKTLMYIA
DVTVNGHPDV KTKDATKKFR EPNVPTFDTI GNYPKGTKDK LEELGREKFS QWLRDEKPVY
FTDTTFRDAH QSLLATRVRT KDIIAVAEGF AKNNPQIFSM EVWGGATFDV SMRFLHECPW
RRLQQLRKAM PNVLLQMLFR GSNGVGYSAY PENLLAKFIE KSAENGIDIF RIFDSLNYVD
AMTPSIKFVR ENTNSLAQAA ISYTGDILKP GKYTLQYYTD LAKRLEDAGA HMLCIKDMAG
LLKPQAATVL VEALKDSVKL PIILHTHDTT SIQAATYLKA IEAGVNVVDC AIASMSGITS
QPNLNSMASI LDGHERSSHL NLSSLNDYSN YWEDVREYYY PFESDMKAGT AQVYENEIPG
GQYSNLRQQA ESLGLGDKLE EIKHNYAVVN ELFGDIVKVT PSSKVVGDMA LFMTANNLSK
ADVLDESKNL AFPSSVHGFF KGELGVPFGG FPEKLQQIVL KGEKPLTGRA NEHLAPVDFD
SDFAAFQLKY PLAEFLDYLS YHMFPKVFDE YYHHAQVYGN VEAIPTPAFF YGLKMGEEIL
ITLSKGKTII VKLLYILPAD ESGMRTVVFE LNGYTRRVQV RDRSVQSSAP VNKKAADPNA
EVGAPLQGKL SKLLVKPGDT VSTNTPLFII EAMKMETTVT ATRDTKIKRI HLPEGTMVQQ
DDLVVELE
//
