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Database: UniProt
Entry: C6BAZ7_RHILS
LinkDB: C6BAZ7_RHILS
Original site: C6BAZ7_RHILS 
ID   C6BAZ7_RHILS            Unreviewed;       621 AA.
AC   C6BAZ7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding {ECO:0000313|EMBL:ACS61255.1};
GN   OrderedLocusNames=Rleg_6512 {ECO:0000313|EMBL:ACS61255.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OG   Plasmid pR132505 {ECO:0000313|EMBL:ACS61255.1,
OG   ECO:0000313|Proteomes:UP000002256}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS61255.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS61255.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|Proteomes:UP000002256};
RC   PLASMID=Plasmid pR132505 {ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain
RT   WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP001627; ACS61255.1; -; Genomic_DNA.
DR   RefSeq; WP_012760748.1; NC_012854.1.
DR   AlphaFoldDB; C6BAZ7; -.
DR   KEGG; rlg:Rleg_6512; -.
DR   HOGENOM; CLU_000395_3_1_5; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000002256; Plasmid pR132505.
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; 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; 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}; Plasmid {ECO:0000313|EMBL:ACS61255.1}.
FT   DOMAIN          1..449
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..322
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          537..617
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   621 AA;  66852 MW;  641D0889C1097270 CRC64;
     MMESLLIANR GEIARRIIRT AKMLGIRTIA VYSEADAGLP FVSEADEAIA IGPSPARESY
     LSQERILDAA RKTGAAAIHP GYGFLSENAG FAEAVEKAGI IWVGAPPAAI RAMGLKDAAK
     ELMQAAGVPV TPGYIGADQS EERLTAEADI IGYPVLIKAV AGGGGKGMRR VDRPQDFAEL
     LASCRREAAA AFGDDRVLIE RYIANPRHIE VQVFADKLGN CVHLFERDCS LQRRHQKVIE
     EAPAPGLDAA TRAVICDAAV KAARAVNYVG AGTIEFIADA SEGLREDRIW FMEMNTRLQV
     EHPVTEAITG EDLVLWQLKV ASGEPLPKMQ DEIAMNGWAF EARLYAENPA AGYLPSIGRL
     EHLRLPETVR VDSGVEQGDD ITAFYDPMIA KVIAHGPNRE AALSKLAAAC AGIEVWPVRS
     NAGLLARIAI DPDFRAARID TGFLDRHDER LVATEPSETA IDSAATALLK NTDGNPWTAL
     TGFRIAGAED KRVRIRIGDH LHWGQSRPEF EANTITIGET TVLFEAGNAW PISLPVASEV
     EASQSAGDGA ILSPMPGLVI SVDVADGDRV AKGDRLLTVE AMKMEHSLRA PFDGIVEKLQ
     VSSGIRVSEN QLVVSIVKEQ D
//
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