(data stored in ACNUC7421 zone)

SWISSPROT: Q13I48_PARXL

ID   Q13I48_PARXL            Unreviewed;      1033 AA.
AC   Q13I48;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   SubName: Full=Putative carbamoyl-phosphate synthase/carboxyltransferase {ECO:0000313|EMBL:ABE36241.1};
DE            EC=6.4.1.1 {ECO:0000313|EMBL:ABE36241.1};
GN   ORFNames=Bxe_C0325 {ECO:0000313|EMBL:ABE36241.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36241.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36241.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36241.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR   EMBL; CP000272; ABE36241.1; -; Genomic_DNA.
DR   RefSeq; WP_011493501.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0325; -.
DR   EnsemblBacteria; ABE36241; ABE36241; Bxe_C0325.
DR   GeneID; 4009839; -.
DR   KEGG; bxb:DR64_8108; -.
DR   KEGG; bxe:Bxe_C0325; -.
DR   PATRIC; fig|266265.5.peg.8102; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG4770; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   HOGENOM; HOG000071838; -.
DR   OMA; VVSGRCF; -.
DR   OrthoDB; 886663at2; -.
DR   BioCyc; BXEN266265:BXE_RS38280-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
DR   PRODOM; Q13I48.
DR   SWISS-2DPAGE; Q13I48.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Ligase {ECO:0000313|EMBL:ABE36241.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000313|EMBL:ABE36241.1}.
FT   DOMAIN        1    437       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      118    315       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      432    509       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      514    787       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000259|PROSITE:PS50980}.
FT   DOMAIN      788   1019       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000259|PROSITE:PS50989}.
SQ   SEQUENCE   1033 AA;  109127 MW;  298FFFFA914FA942 CRC64;
     MSRVLIANRG EVAVRIVRAA KSVGLQTVGI HTPEEANALH VRDSDIAVAL AGVGTAAYLD
     IASIIAAAVR TNCSFIHPGY GFLSESAAFA RACEQAGVTF IGPSPDTLDV FGDKASTREL
     AIRLDVPVLP ATAGLADDAS ALSFMQSLAA PVIVKAVAGG GGRGMRIVTD PTDLPAALSR
     CRSEAERGFG RDDVYVERYL PRSRHIEVQV IGDGSSVVHL GTRDCSLQSR HQKVIEIAPA
     PWLPVEIEEA LLEHALQLAR AVQYRGAGTM EFLIDVDNPS HYYFIEGNPR LQVEHGITEL
     VTGLDIVALQ FAIARGRSLA DEGITQDNVV TSGVAVEARV TLTTPGTIAR FVSPGKGRVD
     SGAYDGLAVG SGFDPLLAKV MVHEPDYPRC ICALADSLGE LVVEGPATNR DGLLSLLADP
     RVRAGDITTT LIDDLPAASA TALVSKVAGS VIAVLARPGE PLRRGQPIVV VEAMKMEHEV
     VAPAAGRLEE MLVAVGQQIT TGQRVASMGY SGAEAEHDAA PGEPAARADL AENLRRHSIT
     LDEARPEAVA SRHARHKRTA RENVADLVDP GSFVEYGALV IAAQRRRRTV EDLELNTPAD
     GLVAGFGTVN GQQIAVLAYD YSVLAGTQGV QSHKKAERLF ELARRRHAPV VIFAEGGGGR
     PGDIDNAAKA TGMDLGTFVA LGRLNGRVPT VAIASGRCFA GNAALVGACD LVIATADANI
     GMGGPAMIEG GGLGRVESRD IGPAARQFEN GVVDVLVADE AEATASAKKY LSYFHAAKRN
     WTAGEQQHLR TIVPEARSRP FDVLRVIQVL SDDDAVLELR AGFGRGIITC LVRIEGVAIG
     IVANNGLHLG GAIDSDSADK MARFLALCDT YSLPIVSLCD TPGFMVGPAS EETAAVRHFG
     RLLVAGPNLS VPLCTVVIRK AWGLGGQAMA GGGFRVPDAI VAWPTAEFGA MGPEGAVRLG
     FRRELEAIAD PVARDAEFDR LVKDYVRDGR GYNAASAFEI DDVIDPADTR RWILATVNRA
     EPIPPTRRHL DTW
//

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