ID A0A0X8FMH6_9LACT Unreviewed; 1143 AA.
AC A0A0X8FMH6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AWM75_02880 {ECO:0000313|EMBL:AMC00034.1};
OS Aerococcus urinaehominis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=128944 {ECO:0000313|EMBL:AMC00034.1, ECO:0000313|Proteomes:UP000062260};
RN [1] {ECO:0000313|EMBL:AMC00034.1, ECO:0000313|Proteomes:UP000062260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG42038B {ECO:0000313|EMBL:AMC00034.1,
RC ECO:0000313|Proteomes:UP000062260};
RX PubMed=27103727;
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT and Aerococcus viridans CCUG 4311T.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000062260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG42038B {ECO:0000313|Proteomes:UP000062260};
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT Illumina Hiseq.";
RL Submitted (JAN-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};
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DR EMBL; CP014163; AMC00034.1; -; Genomic_DNA.
DR RefSeq; WP_067980859.1; NZ_FNHJ01000025.1.
DR AlphaFoldDB; A0A0X8FMH6; -.
DR STRING; 128944.AWM75_02880; -.
DR KEGG; auh:AWM75_02880; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000062260; 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: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; 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|PIRNR:PIRNR001594};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:AMC00034.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062260}.
FT DOMAIN 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 529..797
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1066..1141
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 116
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 538
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 610
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 707
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 736
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 738
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 871
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 707
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1107
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1143 AA; 126665 MW; AFA47E6B71531328 CRC64;
MNKVLVANRG EIAIRVFRAC AELDIATVAI YAKEDELSVH RFKADEAYLV GAGDKPVEAY
LDIEDIIRIA KETGADAIHP GYGFLSENIN FARRCQEEGI IFIGPELDTL DTFGDKMKAK
QAAKAANIAG IPGSDGPVTS VEEVHDFAQE AGFPIIIKAA LGGGGRGMRV VRSEEEIQEN
YEAAISEATK AFGSGVVYVE KYIENPKHIE VQILGDTAGN VMHLWERDCS VQRRHQKVVE
VAPTVSMSQE TREKICGAAR DFMAHIGYVN AGTVEFLLDG EDFYFIEVNP RVQVEHTITE
QITGVDIVQA QIQIAAGKTL QEIGIPKQED LPLMGYAIQC RITTEDPKQG FLPDTGKINT
YRSPGGFGIR LDAGNGFQNA VVTPYYDSML TKLISHAMTF DQAVKKMNRA LREYRIRGVK
NNIPFMRKVL DHPTFQSGRA TTTFIDQTPA LFDFPSDRYS NRGNKVLQYI ADTTVNGFPG
LEQKEKPLYT KAKVPELEVV DQHGRTAKQV FDQEGVKGLQ NWISQREDVL LTDTTMRDAH
QSLMATRMRT RDMLAAAQAY EAANPYIFSA EVWGGATFDT AYRFLTENPW VRLKQLRAAM
PNTLLQMLFR GSNGVGYTAY PDNVLEAFIQ EASQSGIDIF RIFDSLNWTE QMKRPMQYAK
DAGKIVEAAM CYTGDILDPS RLKYSIQYYV DLAKELQDLG ADIIAIKDMA GLLKPQAAYA
LISELKDQVD LPIHLHTHDT AGNGIMTYAE ASRAGVDIVD VATSALSSST SQPSMTSFYY
ALEDSPRKPD LHVANAQKMN QYWSGVREYY EDFISGLKSP ETEIYKTEMP GGQYTNLQQQ
AKGVGLGDRW NEIKQMYHDV NLLFGDIVKV TPSSKVVGDM ALFMVQNNIS VADFFEKGKN
IDFPESVIEF FQGKLGQPAG GFPEDVQEII LKGAPATTER PGALLESVDF EAVKAELAEK
IKAEPSQQDV LAYIMYPKVF LDYRVKTDRY ADLSIVDTPT FFRGMKVGES VEVEIEKGKV
LLIRLIQIGE VDHAGQRIIW FELNGQRREI VVQDQAASTN VAVRQKADPS NPHHIGATMP
GNILKVAVKA GDSVKAGQVV LITESMKMET TIKAPTAGKV NEVLVQAGDQ VQTGDLLISL
DSE
//
