ID Q120B3_POLSJ Unreviewed; 665 AA.
AC Q120B3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Carbamoyl-phosphate synthase L chain, ATP-binding {ECO:0000313|EMBL:ABE47129.1};
GN OrderedLocusNames=Bpro_5270 {ECO:0000313|EMBL:ABE47129.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OG Plasmid pPol338 {ECO:0000313|Proteomes:UP000001983}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE47129.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000318; ABE47129.1; -; Genomic_DNA.
DR RefSeq; WP_011486108.1; NC_007950.1.
DR AlphaFoldDB; Q120B3; -.
DR KEGG; pol:Bpro_5270; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_4; -.
DR OrthoDB; 8865511at2; -.
DR Proteomes; UP000001983; Plasmid pPol338.
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}; Plasmid {ECO:0000313|EMBL:ABE47129.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 588..663
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 665 AA; 70529 MW; EFBDA334783AC303 CRC64;
MLKKVLIANR GEIACRIART CRKLGLEVAT VHSSADRFAR HVREIGESVE LGGAAPSESY
LNIDAIIAAA KRVGADAVHP GYGFVSENAA FVRALDAAGL TFIGPTADTI ERIGGKASAK
REAARLGVPV IPGSEGGMTD PTEVLRLVRG MTLPVLLKAV AGGGGRGMAV VETLEGLEGR
IESAMREAEK SFGNGELIVE RYLPQVRHLE VQVAGDGQGH AIHLFERECT LQRRHQKVIE
EAPSSGLSPK LRAAILADAV KLAAGVNYRG LGTVEFVVTG GEHYFLEVNP RLQVEHPVTE
EVTGLDLVEL QLHIAATGNL PLAQADVHCT GHAFEARLCA EDADAGFLPA TGRLQVVDFS
RAGVRIESGV DSGDEISPHY DSMIAKLIAH ASDRDSARRA LVAGLRESTV IGLVTNLEFL
HELLEWPETR DASFHTRLID ERHAQRGVVA PAAPPIEHLA AAALHWLAQQ RAGWSALGCW
TLWDGFTGWR LSSGPIQAAP QPALVLKAGV AEWPVRFSRR DAQGACTLVI GEQEVNASLQ
PLAAGRSLLH CDGRALELTI RGDARQVELS SALGSGVFTA QPYLGGAAGD AAASGQLGAP
MMGKVVAVKA AVGETVALGQ TVIVLESMKM ELHVTAPFEG SLSSLRCRVG DMVERHQMLA
EVSPS
//
