ID A0A1G8LSX8_9MICC Unreviewed; 857 AA.
AC A0A1G8LSX8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
DE Flags: Fragment;
GN ORFNames=SAMN04488693_1151 {ECO:0000313|EMBL:SDI58794.1};
OS Arthrobacter subterraneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=335973 {ECO:0000313|EMBL:SDI58794.1, ECO:0000313|Proteomes:UP000199258};
RN [1] {ECO:0000313|EMBL:SDI58794.1, ECO:0000313|Proteomes:UP000199258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP_1H {ECO:0000313|EMBL:SDI58794.1,
RC ECO:0000313|Proteomes:UP000199258};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNDT01000015; SDI58794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8LSX8; -.
DR STRING; 335973.SAMN04488693_1151; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000199258; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 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; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF02785; Biotin_carb_C; 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 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; 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; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Pyruvate {ECO:0000313|EMBL:SDI58794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199258}.
FT DOMAIN 1..178
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 2..45
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 252..521
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SDI58794.1"
SQ SEQUENCE 857 AA; 92146 MW; 89541C9B9762B688 CRC64;
LVDTVGERAG QHVFIEMNPR IQVEHTVTEE VTDVDLVQSQ LRIAAGETLA DLGLSQDSVR
LRGAALQSRI TTEDPANGFR PDVGKITAYR SAGGAGVRLD GGTVYAGAEI SPHFDSMLVK
LTCRGRDYES AVRRARRALA EFRVRGVSTN ISFLQAVLDD PDFIAGNVAT SFIDERPELL
TARVPADRGT KLLNWLADVT VNKPHGELTV ELDPAEKLPA VTEAEQRPGS RQRLQELGPE
GFAAELRAQT ALAVTDTTFR DAHQSLLATR VRTRDLVAAG KAVSAKMPDL LSVEAWGGAT
YDVALRFLGE DPWERLAALR AEMPNICLQM LLRGRNTVGY TPYPEAVTKA FVQEAAATGI
DIFRIFDALN DVSQMEPAIR AVRETGTAVA EVALCYTSDM LDPEEKLYTL DYYLDLAQRI
VDAGAHILAI KDMAGLLRPA AAAKLVTALR DRFDLPVHLH THDTAGGQLA TLLAASNAGV
DAVDVASASL AGTTSQPSAS ALVAALAHTD RDTGMSLENV SSLEPYWEAV RRVYAPFESG
LPGPTGRVYR HEIPGGQLSN LRQQAIALGL GERFEAVEDM YTAADRMLGR LVKVTPSSKV
VGDLALQLVG SNVEPAAFEE NPQKYDIPDS VIGFLSGELG DPPGGWPEPF RTKALQGRTV
KVRDAELSAE DQQALDGDSA TRRATLNRLL FEGPTRDFQT TRHTFGDVSV LDTRDYLYGL
QQGSEHVIQL EKGVRLIATL EAVSDADERG MRTVMCTLNG QMRPVVVRDR SVHTDVKAAE
KADPAQPGHV AAPFAGAVTL GVAEGDTVQA GDTVATIEAM KMEAGITTTV GGTIKRLAIS
TIEQAQGGDL LLVIDPK
//
