CARB_RHILO
ID CARB_RHILO Reviewed; 1167 AA.
AC Q98I87;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN Name=carB {ECO:0000255|HAMAP-Rule:MF_01210}; OrderedLocusNames=mlr2517;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01210};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_01210}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
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DR EMBL; BA000012; BAB49629.1; -; Genomic_DNA.
DR RefSeq; WP_010910981.1; NC_002678.2.
DR AlphaFoldDB; Q98I87; -.
DR SMR; Q98I87; -.
DR STRING; 266835.14023021; -.
DR PRIDE; Q98I87; -.
DR EnsemblBacteria; BAB49629; BAB49629; BAB49629.
DR KEGG; mlo:mlr2517; -.
DR PATRIC; fig|266835.9.peg.2024; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_5; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 48855at2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR033937; MGS_CPS_CarB.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 3.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Repeat.
FT CHAIN 1..1167
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145032"
FT DOMAIN 184..380
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 748..960
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 1032..1167
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..455
FT /note="Carboxyphosphate synthetic domain"
FT REGION 456..619
FT /note="Oligomerization domain"
FT REGION 620..1031
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 1032..1167
FT /note="Allosteric domain"
FT BINDING 211..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 774..852
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 919
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 931
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 931
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 933
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1167 AA; 125965 MW; A144AE27D9859849 CRC64;
MPRRTDIKSI LIIGAGPIVI GQACEFDYSG TQACKALKEE GFRVILVNSN PATIMTDPEL
ADATYIEPIT PEVVAKIIAK ERPDALLPTM GGQTALNTAL SLRRMGVLDR YNVEMIGADA
TAIDKAEDRA LFREAMSKIG LETPKSMLAN ATDVKNADRK THEAERAALK AEKPDNLDAE
LDALETRWNL GEGDRKQRYI SHAMAIAAQA LDHVGLPAII RPSFTMGGTG GGIAYNRAEF
YDIVQSGLDA SPTTEVLIEE SVLGWKEYEM EVVRDKADNC IIVCSIENID PMGVHTGDSI
TVAPALTLTD KEYQMMRNAS IAVLREIGVE TGGSNVQFAV NPADGRLVVI EMNPRVSRSS
ALASKATGFP IAKIAAKLAV GYTLDELEND ITGGATPASF EPSIDYVVTK IPRFAFEKFP
GAEPVLTTAM KSVGEVMAIG RTFQESLQKA LRGLETGLTG LDEIEIPGLG HGATVANHAD
DRNAIRAALG TPTPDRLRMV AQAIRMGTSL EDVHAMCKID PWFLEQIAGI LAMEARIREH
GIPQDAVNLR MLKAMGFSDA RLASLTRTDA EVVTKIREKL DVHPVYKRID TCAAEFASPT
AYMYSTYEVP FAGALANEAQ VSSRKKVVIL GGGPNRIGQG IEFDYCCCHA AFALRDAGYE
AIMINCNPET VSTDYDTSDR LYFDPLTAED VLEILRAEQA SGELLGVIVQ FGGQTPLKLA
DALEKAGIPI LGTSPDMIDL AEDRDRFQKL LHKLGLSQPK NGIAYSVEQA RLVAGELGFP
LVVRPSYVLG GRAMQIIHDE SMLQSYLLDT VPGLVPEDIK QKYPNDKTGQ INTLLGKNPL
LFDTYLSGAI EVDVDCLCDG KATFVSGILE HIEEAGIHSG DSACSLPVHS LPSELVDELE
RQTAALARAL NVGGLMNVQY AIKDGTVYVL EVNPRASRTV PFVAKTIGRP IAKIAARIMA
GETLEDAFAH YGAMPDPRNP GHIAVKEAVF PFARFPGVDI LLGPEMRSTG EVMGLDRDFA
LAFAKSQLGA GVDLPRSGTL FVSVRDEDKK GILPAVKRLA GLGFKVLATS GTQRFLAENG
VVAEKINKVL EGRPHIEDAI RNRQVQIVFN TTDGQKAVSD SKSLRRATLM QKVPYYTTLS
GAAAVAEAIA ALKAGSLEVR PLQEYFA
