ID K2ISL8_9RHOB Unreviewed; 1147 AA.
AC K2ISL8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=B30_04192 {ECO:0000313|EMBL:EKE73231.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE73231.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE73231.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE73231.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) 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:EKE73231.1}.
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DR EMBL; AMRK01000002; EKE73231.1; -; Genomic_DNA.
DR RefSeq; WP_009570772.1; NZ_AMRK01000002.1.
DR AlphaFoldDB; K2ISL8; -.
DR STRING; 1208323.B30_04192; -.
DR PATRIC; fig|1208323.3.peg.864; -.
DR eggNOG; COG1038; Bacteria.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006762; 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:EKE73231.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006762}.
FT DOMAIN 3..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 534..802
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1072..1147
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1060..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 543
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 615
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 712
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 741
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 876
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 712
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1113
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1147 AA; 125985 MW; 184A38B444F587E5 CRC64;
MANFKKVLIA NRGEIAIRVM RAANEMGKRT VAIYAEEDKL SLHRFKADEA YKIGEGMGPV
AAYLSIEEII RVAKLSGADA IHPGYGLLSE NPDFVDACTE AGITFIGPKA KTMRQLGDKA
SARKVAIKAG VPVIPATDVL GDDWDAIRKE ATEIGFPLML KASWGGGGRG MRPIMNAEEL
EEKVKEGRRE AVSAFGNGEG YLEKMIIRAR HVEVQILGDS QGNIYHLYER DCSVQRRNQK
VVERAPAPYL SETQREEICN LGKRICEHVN YECAGTVEFL MDMDTGKFYF IEVNPRVQVE
HTVTEEVTGI DIVRAQILIA EGKSLVEATG VASQYDVKLD GHALQCRVTT EDPTNNFIPD
YGRITTYRSA TGMGIRLDGG TAYSGAVITR YYDSLLTKVT AWAPTPEAAI ARMDRALREF
RIRGVSTNIA FVENLLKHPI FLGNEYTTKF IDETPSLFDF KPRRDRATKI LTYLSEITVN
GHPETLGRAK PAADARQPVI PALRVETPVP GTRQLLDEKG PQAVADWMLA QPQLLITDTT
MRDGHQSLLA TRMRSIDMIN AAPAYAANLP GLFSVECWGG ATFDVAYRFL QECPWQRLRD
IREKMPNLMT QMLLRASNGV GYTNYPDNVV QSFVKQAAET GVDVFRVFDS LNWVENMRVA
MDAVIESGKV CEGTICYTGD LFDPARAKYD LKYYVQMGKD LKAAGAHVLG LKDMAGLLKP
AQARVLVKAL KEEVGLPIHF HTHDTSGAAA ATILAAADAG VDAIDAAMDA FSGGTSQACL
GSIVEATRFT ERDTGLDISA IRELSNYWEA VRGQYAAFES GLKAPASEVY LHEMPGGQFT
NLKAQARSLG LEEKWHEVAQ AYADVNMMFG DIVKVTPSSK VVGDMALMMV SQGLTRAQVE
DPKHDVAFPE SVIDMMRGNL GQPPKGFPDA ILKKVLGKEK PNLERPGKHL PPVDIEATRA
ELAAKFEDCV IDDEDLNGYL MYPKVFTDYM DRHDQFGPVR TLPTKNFFYG MEMGEEISVS
IDPGVTLEIR CQALGEPDEK GEVKLFFELN GQPRTVRVKD RSAASTTTAR PKAELGNPKH
IGAPMPGVVA TVAVVAGQKV KKGDVLLTIE AMKMETSINA DQDGVIKAVN VSPASQIDAK
DLLVEFE
//
