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Database: UniProt
Entry: B1J6Q8_PSEPW
LinkDB: B1J6Q8_PSEPW
Original site: B1J6Q8_PSEPW 
ID   B1J6Q8_PSEPW            Unreviewed;       650 AA.
AC   B1J6Q8;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding {ECO:0000313|EMBL:ACA72313.1};
GN   OrderedLocusNames=PputW619_1809 {ECO:0000313|EMBL:ACA72313.1};
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA72313.1};
RN   [1] {ECO:0000313|EMBL:ACA72313.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W619 {ECO:0000313|EMBL:ACA72313.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Psuedomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA72313.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1J6Q8; -.
DR   STRING; 390235.PputW619_1809; -.
DR   KEGG; ppw:PputW619_1809; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_6; -.
DR   OMA; LVKWQLM; -.
DR   OrthoDB; 9763189at2; -.
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   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; IPR048429; MCC_alpha_BT.
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   Pfam; PF21139; MCC_alpha_BT; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SMART; SM01209; GARS_A; 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}.
FT   DOMAIN          5..451
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          124..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          570..649
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   650 AA;  69725 MW;  4499E4A89C840D89 CRC64;
     MSRPPLTTLL VANRGEIACR VMRTAKAMGL TTVAVHSATD RDARHSREAD IRVELGGSKA
     ADSYLVIDKL LAAAKASGAQ AIHPGYGFLS ENAGFARAIE DAGLIFLGPP ASAIDAMGSK
     SAAKALMEAA GVPLVPGYHG DAQDLETFRA AAERIGYPVL LKASAGGGGK GMKVVEEESQ
     LAEALASAQR EAQSSFGDAR MLVEKYVLKP RHVEIQVFAD QHGNCLYLNE RDCSIQRRHQ
     KVVEEAPAPG LSPELRRAMG EAAVRAAQAI GYVGAGTVEF LLDARGEFFF MEMNTRLQVE
     HPVTEAITGL DLVAWQIRIA CGEPLPITQA QVPLIGHAIE VRLYAEDPAN DFLPATGTLT
     LYRESAPGEG RRVDSGVSEG DEISSFYDPM LGKLIAWGEN REQARLRLLA MLDEFAIGGL
     KTNIAFLRRI LAHPAFAAAE LDTGFIPRHQ EVLLPAPQPL PAGFWQAAGK AWLQGQAPHQ
     RDDDSCSPWA ERSGLRLGLP AHSCLHLRSG GECQAIALEQ SVVSAWQLDG EQLGHDEGGV
     RRRYLAVRRG GTLYLRWDGE MHAIEAFDPI AEAEASHSHQ GGLGAPMNGS IVRVLVEPGQ
     VVEAGTALVV LEAMKMEHSI RAPHGGTVKA LFCQEGDMVS EGTVLVELVE
//
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