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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//