ID A0A0H2KXU2_9MICO Unreviewed; 1014 AA.
AC A0A0H2KXU2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
DE Flags: Fragment;
GN ORFNames=FB00_21020 {ECO:0000313|EMBL:KLN32802.1};
OS Cellulosimicrobium funkei.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN32802.1, ECO:0000313|Proteomes:UP000035265};
RN [1] {ECO:0000313|EMBL:KLN32802.1, ECO:0000313|Proteomes:UP000035265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U11 {ECO:0000313|EMBL:KLN32802.1,
RC ECO:0000313|Proteomes:UP000035265};
RA Hu C., Gong Y., Wan W., Jiang M.;
RT "Cellulosimicrobium funkei U11 genome.";
RL Submitted (MAY-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:KLN32802.1}.
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DR EMBL; JNBQ01000069; KLN32802.1; -; Genomic_DNA.
DR RefSeq; WP_047234789.1; NZ_JNBQ01000069.1.
DR AlphaFoldDB; A0A0H2KXU2; -.
DR PATRIC; fig|264251.5.peg.4261; -.
DR Proteomes; UP000035265; 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 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; 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; PS50968; BIOTINYL_LIPOYL; 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 Ligase {ECO:0000313|EMBL:KLN32802.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Pyruvate {ECO:0000313|EMBL:KLN32802.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035265}.
FT DOMAIN 1..336
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 3..203
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 411..680
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 937..1014
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KLN32802.1"
SQ SEQUENCE 1014 AA; 108136 MW; 37B15CDCFE2ABC57 CRC64;
RALKAAREAG LPVLASSEPS SDVDELVAAA DAIGFPVFVK AVAGGGGRGM RRVDTREDLP
ESLAAAMREA DGAFGDPTVF LEQAVLRPRH IEVQILADGA GNVVHLYERD CSLQRRHQKV
VEIAPAPNLD PAIRDALCAD AVRFARHIGY QNAGTVEFLV DTVGERAGQH VFIEMNPRIQ
VEHTVTEEVT DVDLVSAQMR IASGETLEDL GIRQEDVRVN GAALQTRITT EDPANGFRPD
TGRIIAYRSP GGAGVRLDGA TATAGSVVSG HFDSMLVKLT CRGRDFPTAV RRARRALAEF
RIRGIRTNIP FLQAVLADPE FVAGNVATSF IDERPELLAA RESADRGTRL LAYVGDTTVN
RPHGEPRRAT DPATKLPALD LSVAPPPGTR QQLLELGPEG FARALRGEQR LRVTDTTFRD
AHQSLLATRV RTHDLAAVAP HVARATPQLW SVEAWGGATY DVALRFLGED PWERLATLRE
AMPNLAIQML LRGRNTVGYT PYPTRVTEAF VAEAAATGID VFRIFDALND VDQMRPAIKA
VRATGSTVAE VALCYTGNLL DPAEDLYTLD YYLRLADRIV DAGAHVLAIK DMAGLLRPAA
ATRLVTALRE RFDLPVHLHT HDTSGGQMAT LLAAAAAGVD AVDAASAAMA GTTSQPSLSA
LVAGLEHTER DTGLSLTAVA DLEPYWEAVR RVYAPFESGL PGPTGRVYEH EIPGGQLSNL
RQQAIALGLG DKFEQIEAMY AAADRILGRL VKVTPSSKVV GDLALHLVAA GADPAEFAAD
PQAFDIPDSV IGFLGGELGD PPGGWPEPFR SRALAGRAAR GGVTPLSPED EAELAQAGEV
RRRRLNHLLF AGPTKEFEQV RQAYGDVSVL DTPTYLYGLE PGQEVAVALG RGVRLLVGLE
AIGTPDERGM RTVMFTLNGQ LRPIQVRDRA VDVDARTAEK ADPTQPGQVA APFAGAVTPV
VVVGDAVEAG QTVATVEAMK MEAAITTPVA GTVQRVAIGA VQQLEGGDLV LVVG
//
