ID D6KFX0_9ACTN Unreviewed; 607 AA.
AC D6KFX0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:EFF88450.2};
DE Flags: Fragment;
GN ORFNames=SSTG_05845 {ECO:0000313|EMBL:EFF88450.2};
OS Streptomyces sp. e14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF88450.2, ECO:0000313|Proteomes:UP000004704};
RN [1] {ECO:0000313|EMBL:EFF88450.2, ECO:0000313|Proteomes:UP000004704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain e14.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG753629; EFF88450.2; -; Genomic_DNA.
DR AlphaFoldDB; D6KFX0; -.
DR STRING; 645465.SSTG_05845; -.
DR eggNOG; COG1038; Bacteria.
DR Proteomes; UP000004704; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:EFF88450.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000004704}.
FT DOMAIN 209..276
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFF88450.2"
SQ SEQUENCE 607 AA; 64166 MW; 924538E65ECE4CFC CRC64;
CASRPPSASP TPPSATPTSP CSPPGCAPRT SSPSRPSSPA PCPDCSPWSA GAAPPTTSPC
ASSPRTPGSG WRRCARRCPT SASRCCCAAA TPWATRPTRP RSPTPSSRRP PPPASTSSAS
STPSTTSARC GPPSTPYGRP APPPPRSPCA TPPTCPTPPS ASTPWTTTCA WPSRSSRPAH
TCWPSRTWPG CCARPPRPRW SRRCAREFDL PVHLHTHDTA GGQLATYLAA IQAGADAVDG
AVASMAGTTS QPSLSALVAA TDHSERPTGL DLKAVGDLEP YWEGVRRIYA PFEAGLASPT
GRVYHHEIPG GQLSNLRTQA VALGLGDRFE EIEAMYAAAD RILGRLVKVT PSSKVVGDLA
LHLVGAGVAP EDFERSPDRF DIPDSVIGFL RGELGTPPGG WPEPFRTRAL KGRAPAKPVR
ELTDEDRDGL EKTRRTTLNR LLFPGPTREF ETHRQTYGDT GVLDSKDFFY GLRPAKEYAV
DLEPGVRLLI ELQAVGEADE RGMRTVMATL NGQLRPIQVR DRAAASDVPV TEKADRTNPG
HVAAPFAGVV TLAVAEGDEV TAGATVASIE AMKMEAAITA TKDGRVGRLA INRIQQVEGG
DLLMEIA
//
