ID A0A1Q5RPQ6_9BRAD Unreviewed; 1100 AA.
AC A0A1Q5RPQ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:OKO77672.1};
GN ORFNames=AC629_31385 {ECO:0000313|EMBL:OKO77672.1};
OS Bradyrhizobium sp. NAS80.1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1680159 {ECO:0000313|EMBL:OKO77672.1, ECO:0000313|Proteomes:UP000186592};
RN [1] {ECO:0000313|EMBL:OKO77672.1, ECO:0000313|Proteomes:UP000186592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAS80.1 {ECO:0000313|EMBL:OKO77672.1,
RC ECO:0000313|Proteomes:UP000186592};
RA Granada C., Sant'Anna F.H., Passaglia L.;
RT "Genome of Bradyrhizobium sp. NAS80.1.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKO77672.1}.
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DR EMBL; LGHL01000162; OKO77672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5RPQ6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000186592; Unassembled WGS sequence.
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; 117756 MW; B0A2F2A2EE043DAB CRC64;
MSFKKLLIAN RGEIAIRIAR AAADAGIATV AIHPADDALS LHVRVADEAI EIPGRGARAY
LDVDAVVRAA KSAGCDAVHP GYGFLSENAA FAKACADAGI AFVGPKPAAL ELFGDKVAAR
QLAKRCGVPI IAGTSGPSSL EEITAFFHSL GSHAAIVIKA MAGGGGRGMR VVEKAADLAE
AYARCQSEAK AAFGFDGVYA ERLIRQARHI EVQIIGDRHG AISHLWEREC TIQRRHQKLI
EVAPSPSLSD SLRGRIIEAA KQLAAAASYD NLGTFEFLVD GSAEDSFAFI EANPRLQVEH
TVTEEVLGLD LVRAQLAVAA GASLASLGLA QGAIPKPRGY AMQLRVNMET LDELGATHPT
GGVLAVFEPP SGPGVRVDSF GYAGYKTSAA FDSLLAKVIV HTPGETWHDV VAKASRALRE
FRIDGVVTNI AFLQALLAHP DFRTNRIATD FIDRNIAKLV EAADGAAKPL YFAATERTGH
GAEAHVAQAV PEGAVMVAAP LQGTIVTIQV KEGEIVRPGQ QLAVIESMKM EHLVMAEQGG
RVMKLVASDG VTLMHGEPIM YLEPLDVAAD ASATETDIDL DHIRPDLAEL IARQANTLDL
NRPTSVERRR NTNQRTAREN VAQLVDEGSF MEYGSLAIAA QRRRRKLDDL IKNTPADGLV
MGVATVNAEK FGPEAGRCIV VAYDYTVLAG TQGHMNHKKI DRMLTLAEDW RVPLVFYAEG
GGGRPGDTDR LGMTGLDGPS FVQFARLSGL VPVVGVVSGY CFAGNAAMLG CCDVIIATKN
ASIGMGGPAM IEGGGLGVYH PAEVGPVSFQ APNGVIDILV EDEEEATRVA QKYLSYFQGA
VTEWQAADQR LLRRAIPENR LRVYDIRSVI DLVADKDSVL ELRRDYGVGM ITALIRIEGK
PFGLIANNPR HLGGAIDADA GDKAARFLQL CDAFDLPVVS LCDTPGFMVG PEAEKTAIVR
HVSRMFVTGA SLTVPLFGIV LRKGYGLGAQ SMIGGGFHAS FFTAAWPTGE FGGMGFEGYV
RLGFRKEMEA IADPEERETY YRNKVAELYA NGKAVSIASV FEIDNVIDPA ETRRWIMAGL
RSVPKPPART EKKRPCIDTW
//
