ID W5WHQ6_9PSEU Unreviewed; 1125 AA.
AC W5WHQ6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, 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=KALB_7366 {ECO:0000313|EMBL:AHI00724.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI00724.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI00724.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI00724.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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; CP007155; AHI00724.1; -; Genomic_DNA.
DR RefSeq; WP_025360562.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WHQ6; -.
DR STRING; 1449976.KALB_7366; -.
DR KEGG; kal:KALB_7366; -.
DR PATRIC; fig|1449976.3.peg.7399; -.
DR eggNOG; COG1038; Bacteria.
DR HOGENOM; CLU_000395_0_0_11; -.
DR OrthoDB; 9760256at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000019225; Chromosome.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225}.
FT DOMAIN 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 525..794
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1051..1125
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 926..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 534
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 704
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 733
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 735
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 868
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 704
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1091
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1125 AA; 120957 MW; D63EF1AE8648B7E8 CRC64;
MFRKVLVANR GEIAIRAFRA AYELGAGTVA VFPYEDRNSL HRLKADEAYE IGEAGHPVRA
YLSVEEIVEA ARKAGADAIY PGYGFLSENP ELASACQRAG ITFVGPPAEV LELTGNKARA
IAAAKAAGLP VLQSSEPSTD VDALLAAAGQ IGFPIFVKAV AGGGGRGMRR VLDESTLRES
IEAAMREAES AFGDATVFLE QAVVQPRHIE VQILADAEGN VIHLYERDCS VQRRHQKVIE
LAPAPNLDPL VRDKICADAV AFAKQIGYRN AGTVEFLVDR EGRHVFIEMN PRIQVEHTVT
EEVTDVDLVQ SQLRIASGQT LSDLGLSQDA VYLRGAALQC RITTEDPVNG FRPDTGVISA
YRSPGGSGIR LDGGAIGAGS AVGAHFDSML VKLTCRGRNF ETAVARARRA VAEFRIRGVS
TNIPFLQAVL DDADFRGGRV TTAFIEERPH LLTARQSADR GTRLLTYLAD VTVNKPNGPR
PTSVDPREKL PAVDLSAEAP AGSKQKLTEL GPEGFASWMR DSAGVLVTDT TFRDAHQSLL
ATRVRTKDLV QVAPHVARLT PQLLSLECWG GATYDVALRF LAEDPWERLA ALREAAPNLC
LQMLLRGRNT VGYTPYPESV TRAFVEEATE TGIDIFRIFD ALNDIEQMRP AIEAVRETGK
AVAEVSLCYT ADLSDPAEQL YTLDYYLKLA EQIVGAGAHV LAIKDMAGLL RPPAASRLVT
ALRKEFDLPV HLHTHDTAGG QLATYLAAIQ AGVDAIDGAT ASIAGTTSQP SLSAIVAATD
HSARTTGLDL QAVCDLEPYW EAVRKVYAPF ESGLPAPTGR VYHHEIPGGQ LSNLRQQAIA
LGLGDRFEAI EAMYAAADRM LGRLVKVTPS SKVVGDLALH LVGAGVAPAD FEADPGRFDI
PDSVVGFLHG ELGDPPGGWP EPFRSKALRG RSAPKKVTEL SEEDNRGLET DRRGTLNRLM
FPAPTKEFRT HRDAYGDTSV LRSKDFFYGL RPGEEYQVDL ERGVRLLITL EAIGEADERG
MRTVMAVLNG QLRPIQVRDR SVAADVPVAE KADRGNSNHV AAPFAGVVTM AVAEGDTVEA
GQTVATIEAM KMEAGITAPK AGTVQRLAIG SQQQVEGGDL LVVLA
//
