ID E6V7E2_VARPE Unreviewed; 666 AA.
AC E6V7E2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:ADU39511.1};
GN OrderedLocusNames=Varpa_5355 {ECO:0000313|EMBL:ADU39511.1};
OS Variovorax paradoxus (strain EPS).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU39511.1, 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:ADU39511.1, ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|EMBL:ADU39511.1,
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; ADU39511.1; -; Genomic_DNA.
DR RefSeq; WP_013543713.1; NC_014931.1.
DR AlphaFoldDB; E6V7E2; -.
DR STRING; 595537.Varpa_5355; -.
DR KEGG; vpe:Varpa_5355; -.
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; 3.30.700.40; -; 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}.
FT DOMAIN 1..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 584..663
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 666 AA; 72042 MW; 4CA0DC7829B11170 CRC64;
MFKKILIANR GEIACRVAAT ARRMAIRTVA VYSDADAHAN HVRACDESVH IGGSAPKESY
LRWERILEAA KATGAEAVHP GYGFLSENEE FAQACADAGL VFIGPPPSAI KAMGLKAESK
QLMEKAGVPL VPGYHGHDQD PALLQREADR IGYPVLIKAS AGGGGKGMRA VDKAADFEAA
LASCKREAIN SFGDDAVLIE KYVQRPRHIE IQVFGDTHGN YVYLFERDCS VQRRHQKVLE
EAPAPGMTEA MRKQMGDSAV AAARAVNYVG AGTVEFIVEQ REGGEMNFFF MEMNTRLQVE
HPVTEAITGL DLVEWQLRVA SGEVLPAKQA DLQIHGHAIE ARICAENPDN NFLPATGTLR
VYRKPQATAF QRSRVRIDDG VREGGEISPF YDSMIAKLIV HGSTRAEALA RLDAALAQVQ
IVGVATNVQF LRGILATESF SKANLDTALI ERERAVLFDR EALGLPMAAA AAITRTLITE
WPAKMPDPFA RRDGWRALGE YRRHFDFEFR GAEQTAVLTY KRDGGLWLEA GGTAGPLVIG
QFPTGEFEVE FGGSRQTLDV HLDGATAHVF AAKGATKITA IDRLAHAGDT QAEGGRLTAP
MPGKVVSFAV KAGDKVSRGQ PLAVMEAMKM EHTIAAPADG TVEELMFSPG EQVAEGEELL
RMATAA
//
