ID A0A0X8CEW9_9BRAD Unreviewed; 1100 AA.
AC A0A0X8CEW9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:AMA56069.1};
GN ORFNames=BCCGELA001_07230 {ECO:0000313|EMBL:AMA56069.1};
OS Bradyrhizobium sp. CCGE-LA001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA56069.1, ECO:0000313|Proteomes:UP000019052};
RN [1] {ECO:0000313|EMBL:AMA56069.1, ECO:0000313|Proteomes:UP000019052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA56069.1,
RC ECO:0000313|Proteomes:UP000019052};
RX PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT related Phaseolus species.";
RL Mol. Phylogenet. Evol. 79:1-11(2014).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP013949; AMA56069.1; -; Genomic_DNA.
DR RefSeq; WP_060734942.1; NZ_CP013949.1.
DR AlphaFoldDB; A0A0X8CEW9; -.
DR STRING; 1223566.BCCGELA001_07230; -.
DR KEGG; brc:BCCGELA001_07230; -.
DR Proteomes; UP000019052; Chromosome.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF5; BLL7292 PROTEIN; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50989; COA_CT_CTER; 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 2..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 485..563
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 843..1082
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1100 AA; 117652 MW; AA1682C8DB579AF6 CRC64;
MSFKKLLIAN RGEIAIRIAR AAADGGITTV AIHPADDALS LHVRVADEAI EIPGRGARAY
LDIDAVVKAA KATGCDAVHP GYGFLSENAA FAKACTEAGV VFVGPKPAAL ELFGDKVAAR
QLAKRCGVPI IAGTSGPSTL EEITAFFTSL GSNAAIVIKA MAGGGGRGMR VVESSADLAE
AYARCQSEAK AAFGFEGVYA ERLIRQARHI EVQIIGDHHG AISHLWEREC TIQRRHQKLI
EVAPSPSLSD SLRSRIIEAA KQLALAASYD NLGTFEFLVD GTADDNFAFI EANPRLQVEH
TVTEEVLGLD LVRAQLAVAS GATLASLGLA RGSIPKPRGY AMQLRVNMET LDETGATHPT
GGVLAVFEPP SGPGVRVDSF GYAGYKTSAA FDSLLAKVIV HTSGEAWHDV VAKATRALRE
FRIDGVVTNI SFLQAVLAHP DFRTNRIATD FIDRNIAKLV EAADGAAKPL YFAAAERSGH
DTEPQVAQAV PEGALMVAAP LQGTIVTIQV KEGEIVRPGQ QLAVIESMKM EHLVMAEQGG
RVMKLVAGDG VTLLHGEPIL YLEPLDVAAD SAAAEADIDL DHIRPDLAEL IARQANTLDA
NRPASVERRR NTNQRTAREN VAQLVDDGSF MEYGSLAIAA QRRRRKLDDL IKNTPADGLV
MGVATVNAEK FGPEGGRCIV VAYDYTVLAG TQGHMNHKKI DRMLTLAEDW RVPLVFYAEG
GGGRPGDTDR LGMTGLDGPS FVQFARLSGL VPVVGIVSGY CFAGNAAMLG CCDVIIATKN
ASIGMGGPAM IEGGGLGVYH PAEVGPVSFQ SPNGVIDILV EDEEEATRVA QKYLSYFQGT
VTNWEAADQR LLRRAIPENR LRVYDIRSVI DLVADKDSVV ELRRDYGAGM ITALIRIEGK
PFGLIANNPR HLGGAIDADA GDKAARFLQL CDAFDLPIVS LCDTPGFMVG PEAEKTAIVR
HVSRMFVTGA SLTVPLFGIV LRKGYGLGAQ SMIGGGFHAS FFTAAWPTGE FGGMGLEGYV
RLGFRKEMEA IADPEERETY YRNKVAELYA NGKAVSIASV FEIDNVIDPA ETRRWIMAGL
RSVPKPPART GKKRPCIDTW
//
