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Database: UniProt
Entry: A1WKK4_VEREI
LinkDB: A1WKK4_VEREI
Original site: A1WKK4_VEREI 
ID   A1WKK4_VEREI            Unreviewed;       675 AA.
AC   A1WKK4;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain, ATP-binding {ECO:0000313|EMBL:ABM58161.1};
GN   OrderedLocusNames=Veis_2415 {ECO:0000313|EMBL:ABM58161.1};
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM58161.1, ECO:0000313|Proteomes:UP000000374};
RN   [1] {ECO:0000313|Proteomes:UP000000374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP000542; ABM58161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1WKK4; -.
DR   STRING; 391735.Veis_2415; -.
DR   KEGG; vei:Veis_2415; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_4; -.
DR   OMA; GRHARCD; -.
DR   Proteomes; UP000000374; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 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   SUPFAM; SSF51230; Single hybrid motif; 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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000374}.
FT   DOMAIN          18..464
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          137..334
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          592..667
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   675 AA;  70973 MW;  0A80030339BE2C97 CRC64;
     MSRDAASGSI RMTGQARPFN TLLVANRGEI AIRIMRTARR LGLRTVAIYS EADRASLHAV
     QADTAVCVGP AAPRESYLNI EAILQAARRT GADAIHPGYG FLAENGDFAA AVTGAGLVFV
     GPPAEAIRAM GNKAEAKRLM RAAGMPCVPG YQGLDQGDPA LQAAASGIGF PVMVKAAAGG
     GGRGMRLVHG SSDLAAALAS ARSEALAAFG SDELILERAL LAPRHIEIQV FADTHGHVIH
     LGERDCSVQR RHQKLIEEAP SPAVGPELRA RMGKAAVDAA NAIGYVGAGT MEFLLDRSGA
     FYFMEMNTRL QVEHAVTEAI TGLDLVEWQL RVAAGEPLPL TQDEVAFDGH AIEARLTAED
     VSAGFLPQGG PVLCWRPPAD GHDVRVDHGL SEGAVVPPDY DSMVAKLVAH ARTRDEARRK
     LHRALQDCVL LGVASNQGFL AECLEHPAFC RGDVDTGFIA EHMGAALAGT CPDSTTVAAA
     ALAAAGWPWH GATRLGHAVV PVDLELGRRR WHVQLQAADD SVDVTVRQEA QVDSQVDSVR
     LALVRKHGDS VWWLEGNGQM QRVVQARNSA GIHLHSAGRA WCFVPVDPRR ARAQDGGSGA
     VTAPLTGRIA AVGVAVGDTV QAGQTLVVLE AMKMEHRLSA PFAGRITELS AQVGGQARAG
     SKLVQVQPLG IGAAA
//
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