CARB_BUCAI
ID CARB_BUCAI Reviewed; 1079 AA.
AC P57244;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Carbamoyl-phosphate synthase large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB; OrderedLocusNames=BU144;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(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;
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.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
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:0000250}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; BA000003; BAB12862.1; -; Genomic_DNA.
DR RefSeq; NP_239976.1; NC_002528.1.
DR RefSeq; WP_010895970.1; NC_002528.1.
DR AlphaFoldDB; P57244; -.
DR SMR; P57244; -.
DR STRING; 107806.10038827; -.
DR EnsemblBacteria; BAB12862; BAB12862; BAB12862.
DR KEGG; buc:BU144; -.
DR PATRIC; fig|107806.10.peg.153; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_3_6; -.
DR OMA; IEPAGIH; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001806; 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: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 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; 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; 2.
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; 2.
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; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..1079
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000144995"
FT DOMAIN 133..328
FT /note="ATP-grasp 1"
FT DOMAIN 679..870
FT /note="ATP-grasp 2"
FT DOMAIN 937..1079
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 2..403
FT /note="Carboxyphosphate synthetic domain"
FT REGION 404..553
FT /note="Oligomerization domain"
FT REGION 554..936
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 937..1079
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 705..762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 841
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 841
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 843
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1079 AA; 120516 MW; 088D77AA95FD4217 CRC64;
MPKSTDIKSI LILGAGPIVI GQACEFDYSG TQACKALKEE GYRIILLNSN PATIMTDPDM
ADATYVEPIH WEIVEKIIQK EKPDALLPTM GGQTALNCAL ELDHKGILKK YGVQIIGATV
DAIKKAENRK LFEHSMKKLN LETAKCGIAH NIQEAFLVLN NVGFPCIIRP SFTMGGHGGG
IAYNHEEFEK ICERGLELSP STELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENLDPM
GIHTGDSITV APAQTLTDKE YQVMRNASMS ILREIGVETG GSNVQFAINP KNGRMIVIEM
NPRVSRSSAL ASKATGFPIA KIAAKLAIGY TLDELANDIT GTNTTASFEP SIDYIVTKIP
RFNFEKFPGC DDRLTTQMKS VGEVMAIGRT FQESIQKAIR GLEVGASGFD SKISSRDSEY
LIKIRRELKD AGSERIWYIG DAFRYGMSIN DVFDLTSIDP WFLVQIKEII LLEKKIIKNG
FIGLKYDFFY FLKRKGFSDQ RIAILTNKNE SEIRQLRYKL NLHPVYKRID TCSAEFSTET
AYMYSTWEDE CESHPSKNNK KIIILGGGPN RIGQGIEFDY CCVHAAQALR EDGFEAIMVN
CNPETVSTDY DISDRLYFEP ITLENVLEIV RIEKPKGVII QYGGQTPLKL AHEFEKEGVP
IIGTSPDSID TAENRYRFQK TVNKLRLQQP LNATVLTLDE AYKKADIIGY PIMVRPSYVL
GGRAMEIVYE PYGLENYFKT TLKKNNTTPI LLDQYLDYAT EVDVDAICDG ETVLIGGIME
HIEQAGVHSG DSACSLPAYT LTSKVQNEIR RQVKKLAFEL SVKGLMNIQF AIKNNKIYII
EVNPRAARTV PFVSKAIGLA LAKISVRVMC GKTLLEQGFI KEIIPPYFSV KEAVLPFDKF
QGVDPILGPE MRSTGEVMGI GKNFSEAFSK SMLGAHTNMK KSGRVLLSVR NNDKNNIINL
AVKLKKLGFK IDATKGTSVA LKKSGISSRL VNKVHEGRPH IQDRLKNGEY SYIVNTTSCY
QGIKDSKLIC RSALQYKVHY DTTVNGAFAT VMALNENPIK NIETLQKIHK KIQLFYTKK
