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
//