ID E6V2C7_VARPE Unreviewed; 650 AA.
AC E6V2C7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:ADU34558.1};
GN OrderedLocusNames=Varpa_0336 {ECO:0000313|EMBL:ADU34558.1};
OS Variovorax paradoxus (strain EPS).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34558.1, ECO:0000313|Proteomes:UP000008917};
RN [1] {ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Orwin P., Han J.-I.G., Woyke T.;
RT "Complete sequence of Variovorax paradoxus EPS.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU34558.1, ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|EMBL:ADU34558.1,
RC ECO:0000313|Proteomes:UP000008917};
RX PubMed=24158554;
RA Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT "Genome of the Root-Associated Plant Growth-Promoting Bacterium Variovorax
RT paradoxus Strain EPS.";
RL Genome Announc. 1:e00843-e00813(2013).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP002417; ADU34558.1; -; Genomic_DNA.
DR RefSeq; WP_013538804.1; NC_014931.1.
DR AlphaFoldDB; E6V2C7; -.
DR STRING; 595537.Varpa_0336; -.
DR KEGG; vpe:Varpa_0336; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_4; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000008917; 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; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 3..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 570..648
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 650 AA; 68637 MW; 53D07243696E7C1F CRC64;
MKGFNKILIA NRGEIAVRVM RTARTMGYRT VAVYSSADAD AEHVRQADQA VWIGESLPAQ
SYLNIAAIIE AARASGAQAV HPGYGFLAEN AGFAEACRNA GLVFIGPSPE AIRAMGDKAG
AKRLMRAAGV PCIPGYQGED QSQSTLAAEA ARIGWPVMIK ATAGGGGRGM RLVPSAAAFA
DLLQSAQSEA LNAFGNATVI LERAVVAPRH IEIQVFADRH GNGIHLGERD CSVQRRHQKV
IEESPSPAVS AELRERMGAT AVAAAKAIAY EGAGTLEFLL DADGQYWFME MNTRLQVEHP
VTEAVTGLDL VELQLRVAAG EPLPLTQQDV QMNGHAIEVR LCAEDPQQGF MPQSGTLAAW
RPSPALRIEH ALRDGAEVPA FYDSMIAKLV SHGRTRDEAR QRLIAGLQDT VALGIATNQE
FLRRALSHPV FAEGAATTAF IAEHAEALLA PDAAMEGRAA LLAALLLQLG ERGWPSPLAH
TLPNALRFSL NGEVHAARVT PQGAGRFDVA VDATGPERIE LLALPGDGVV RFSCGGVSEQ
AMSVRKSATH LWIHFSGQAF ELENLTHVAV PRAGAAGGDG LLRASMNGRV IALLAAEGDT
VAAGQPLVTL EAMKMEHVHC APRAGRVAAL HVAVGAQVAA RHVVAEIADA
//
