ID A0A0D0L6Z7_9NOCA Unreviewed; 756 AA.
AC A0A0D0L6Z7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:KIQ08181.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:KIQ08181.1};
DE Flags: Fragment;
GN ORFNames=RU01_21010 {ECO:0000313|EMBL:KIQ08181.1};
OS Rhodococcus sp. MEB064.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1587522 {ECO:0000313|EMBL:KIQ08181.1, ECO:0000313|Proteomes:UP000032087};
RN [1] {ECO:0000313|EMBL:KIQ08181.1, ECO:0000313|Proteomes:UP000032087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEB064 {ECO:0000313|EMBL:KIQ08181.1,
RC ECO:0000313|Proteomes:UP000032087};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:KIQ08181.1}.
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DR EMBL; JXQS01000073; KIQ08181.1; -; Genomic_DNA.
DR RefSeq; WP_042576519.1; NZ_JXQS01000073.1.
DR AlphaFoldDB; A0A0D0L6Z7; -.
DR Proteomes; UP000032087; 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:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B 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; 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 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; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00682; HMGL-like; 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; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KIQ08181.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:KIQ08181.1}.
FT DOMAIN 1..449
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 524..756
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT NON_TER 756
FT /evidence="ECO:0000313|EMBL:KIQ08181.1"
SQ SEQUENCE 756 AA; 82135 MW; C46E0ACE9A36EE6B CRC64;
MFSKVLVANR GEIAIRAFRA AYELEAQTVA VFPFEDRNSV HRTKADEAYE IGEPGHPVRN
YLSVDLIVDA AKRSGADAIY PGYGFLSENP ELAAACAEAG ITFVGPSAQV LELTGNKARA
IAAAKDAGLP VLASSEPSTD VDALVAASES MTFPVFVKAV AGGGGRGMRR VAEPSGLREA
IEAAAREAES AFGDATVFLE QAVVEPRHIE VQILADTHGN VMHLFERDCS VQRRHQKVVE
LAPAPNISDE LRARLCSDAV AFARKIGYSC AGTVEFLVDR DGNHVFIEMN PRIQVEHTVT
EEITDVDLVQ SQLRIASGES LEDLGLRQED IRIRGAAMQC RITTEDPANG FRPDTGRITA
YRTPGGAGIR LDGGTTLGAE VSAYFDSMLV KLTCRGRTFE DAVARSRRAL AEFRIRGVST
NIGFLQGLLQ DEDFRAGNVT TSFIEERPEL LTARSSGDRG TKILTYLADV TVNKPHGERP
STVYPQDKLP DIDLSVAPRD GSRQRLLELG PEGFARDLRQ RKALGVTDTT FRDAHQSLLA
TRVRTSGLLM VAPYVARTTP ELLSIECWGG ATYDVALRFL HEDPWERLAA LREAVPNIAL
QMLLRGRNTV GYTPYPERVT TAFVEEAAAT GVDIFRIFDA LNNVDQMRPA IDAVRETGTT
IAEVAMSYTG DLSNPDEKLY TLDYYLRLAE QIVDAGAHVL AIKDMAGLLR APAAATLVSA
LRKNFDLPVH VHTHDTPGGQ LATYLAAWEA GADAVD
//
