ID A0A1M6EQ26_9BACT Unreviewed; 1149 AA.
AC A0A1M6EQ26;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN02745146_1769 {ECO:0000313|EMBL:SHI87458.1};
OS Hymenobacter daecheongensis DSM 21074.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1121955 {ECO:0000313|EMBL:SHI87458.1, ECO:0000313|Proteomes:UP000184418};
RN [1] {ECO:0000313|EMBL:SHI87458.1, ECO:0000313|Proteomes:UP000184418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21074 {ECO:0000313|EMBL:SHI87458.1,
RC ECO:0000313|Proteomes:UP000184418};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQYN01000003; SHI87458.1; -; Genomic_DNA.
DR RefSeq; WP_073107889.1; NZ_FQYN01000003.1.
DR AlphaFoldDB; A0A1M6EQ26; -.
DR STRING; 1121955.SAMN02745146_1769; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000184418; 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:SHI87458.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184418}.
FT DOMAIN 2..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 535..805
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1074..1149
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 295
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 202
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 715
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 744
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 746
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 879
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 715
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1115
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1149 AA; 128973 MW; BF313B91D7B93566 CRC64;
MNIRKLLVAN RGEIAIRVLR AATELGIPTV AIYTYEDRYS LHRYKADEAY QIGRDDDPLK
PYLDIEGILR VAKENGIDAI HPGYGFLSEN ATLARRCAEE GITFIGPRPE VMEALGDKVA
AKRVAVQCQV PIIESSQQDL TDFDIAKAEA NRIGYPVMLK AASGGGGRGM RIIRDDEQLE
RGFFEAKNEA LNAFGDDTVF LEKYVERPKH IEVQIVADNY GNIVHLYERD CSVQRRFQKV
VEVAPSLDLA DHQRHLLYEY ALRICRAVNY NNVGTVEFLV NPELDRIYFI EVNPRIQVEH
TVTEMITGID LIKTQIYIAD GARLSAPEIG LEVGGRPLKT GYAIQCRITT EDPENDFKPD
YGTIVAYRSA GGFGIRLDQG SVYQGAKISP FFDSLLVKVS AHAPTLEGAA SKMARTLDEF
RIRGVRTNIQ FLQNIIAHPE FVSGHANVDF IKDHPELFRY KARQDRGTKV LNFVGDLIVN
GNPDVKGLID PKKELRKPKL PHFDPLAAYQ PGTKDKLTEL GPEGFAKWLR EDPLIHYTDT
TFRDAHQSLL ATRMRTFDMV KVAERYAKMH PQTFSMEVWG GATFDVALRF LHEDPWERLA
KIRTAVPNIL LQMLIRGANG VGYKAYPDNL TERFVQQAWE TGVDVFRIFD SLNWMPGMES
CINFVRKKTK GLAEASICYT GDILDPKRNQ KYSLDYYLRL ARQIEDAGAH ILCIKDMAGL
LKPYAATELI AGLRDTVKIP IHLHTHDTSS LQPATYLKAV EAGVNVIDVA LGALSGLTSQ
PNFNSVVEMF RGTPRHREFD QDSLNDFSNY WETVREYYYP FESGLKAGTS EVFQHEIPGG
QYSNLRPQAA ALGLSDKFEQ VKKTFAEVNE LFGDIVKVTP SSKVVGDMAL FLVTNNLTAA
DVLEKGHALS FPESVQSLFR GDIGQPEGGW PKEVQKLILK DEKPFTDRPN EHLKPIDFKK
EMKAFEAKFG PGGKFTDLLS WLLYPKVFEQ YWAHLQEFGD VSVVPTRVFF YGLKPGEETI
IDIARGKSVI VKLRSVGEVN DDGCRTVFFS FNGQTRNLEV RDRSVEVKTI RNQKIDRANP
KQVGAPLQGM LSKMLVASGQ QVSRNTPLFV IEAMKMETTI TAPADTTVQN LHLGEGTLVN
ADDLVLTLG
//
