ID Q212E4_RHOPB Unreviewed; 664 AA.
AC Q212E4;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Carbamoyl-phosphate synthase L chain, ATP-binding {ECO:0000313|EMBL:ABD88742.1};
GN OrderedLocusNames=RPC_3200 {ECO:0000313|EMBL:ABD88742.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88742.1};
RN [1] {ECO:0000313|EMBL:ABD88742.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD88742.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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; CP000301; ABD88742.1; -; Genomic_DNA.
DR AlphaFoldDB; Q212E4; -.
DR STRING; 316056.RPC_3200; -.
DR KEGG; rpc:RPC_3200; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_5; -.
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; 3.30.470.20; 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}.
FT DOMAIN 11..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 130..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 583..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 664 AA; 70494 MW; E5AB41193E549E41 CRC64;
MSVAPALQLT PFSSILIANR GEIALRIMRT ARKLGYAVVA VYSDADADAL HVRAADAAVR
IGGALPQQSY LNIEAIIAAA KQSGADAVHP GYGFLAENQD FAAACRDAGL LFIGPSAASI
AAMANKAGAK AIMRKAGVPC VPGYQGADQS DEAMAREAAS IGFPVMIKAV AGGGGRGMRL
VEDAAAFAEA LRGARSEAQG GFGDPTVILE RAIVNPRHIE IQVFGDRYGH AVHLGERDCS
VQRRHQKLIE EAPSPAVSQA LREEMGTVAV NAAKAIGYEG AGTLEFLLDG DGRFYFMEMN
TRLQVEHPVT EAITGLDLVE LQLRIAAGEP LPLQQDDVQF RGHAIEVRLC SEDPAQDFMP
QSGRLALWQM PGELRVEHAL QSGSAISPYY DSMIAKIVAH GDSRDEARRK LLHGLARTVA
FGVSTNCSFL AACLRHPSFA AGAATTGFIA QHRDALLAPE PDHDVPAAAV AALLLYVTDR
HAPRWRKGRS LAATFPCPLR IEIDGITLEP EVTRERDGCT IVRIGGNAVR FALDELSGDT
LRFRADGMSE SIVYHRDGDA LFVLRQGVTS AVRDLTRAAP ARAAAAGGDG RLRAAMNGRV
VAVLVKPGDQ VEAGQPVLTL EAMKMEHVHA APISGIVSAI DVEEGEQVTT GRIVAEIEAM
SQQA
//
