CARB_BACCL
ID CARB_BACCL Reviewed; 1065 AA.
AC P46537;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=pyrAB;
OS Bacillus caldolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 405 / NBRC 15313 / YP-T;
RX PubMed=7516791; DOI=10.1099/00221287-140-3-479;
RA Ghim S.Y., Nielsen P., Neuhard J.;
RT "Molecular characterization of pyrimidine biosynthesis genes from the
RT thermophile Bacillus caldolyticus.";
RL Microbiology 140:479-491(1994).
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: 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 -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; X73308; CAA51739.1; -; Genomic_DNA.
DR PIR; I40169; I40169.
DR AlphaFoldDB; P46537; -.
DR SMR; P46537; -.
DR UniPathway; UPA00070; UER00115.
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; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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 ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT CHAIN 1..1065
FT /note="Carbamoyl-phosphate synthase pyrimidine-specific
FT large chain"
FT /id="PRO_0000144986"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT DOMAIN 671..861
FT /note="ATP-grasp 2"
FT DOMAIN 930..1065
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT REGION 402..546
FT /note="Oligomerization domain"
FT REGION 547..929
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 930..1065
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 697..754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1065 AA; 116483 MW; 4FEA3A94BBBDB4B1 CRC64;
MPKRRDIETI LVIGSGPIVI GQAAEFDYAG TQACLALKEE GYKVILVNSN PATIMTDTEI
ADKVYMEPLT LDFVARIIRK ERPDAILPTL GGQTGLNLAV ELAKAGVLEE CGVEILGTKL
EAIEKAEDRE QFRALMNELG EPVPESAIIH SLEEAYAFVE QIGYPVIVRP AFTLGGTGGG
ICTNEEELVE IVSTGLKLSP VHQCLLERSI AGYKEIEYEV MRDANDNAIV VCNMENIDPV
GIHTGDSIVV APSQTLSDRE YQLLRNASLK IIRALGIEGG CNVQLALDPD SFRYYVIEVN
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMINPVTG KTYACFEPAL DYVVTKIPRF
PFDKFESANR RLGTQMKATG EVMAIGRTFE ESLLKAVRSL EIGVHHLELN EAKTAADDVM
EKRIRKAGDE RLFYIAEALR RGVTVETLHE WSQIDRFFLH KIQNIIEMET VLKNHPGDLD
VLKKAKGLGF SDAAIAALWN KTERDIYAVR RQRGIMPVYK MVDTCAAEFT SETPYYYSTY
EEENESIVTE KPSVIVLGSG PIRIGQGIEF DYATVHCVWA IKQAGYEAII INNNPETVST
DFSTSDKLYF EPLTAEDVMH VIDLEQPIGV IVQFGGQTAI NLAAELEARG VRLLGTTLED
LDRAEDRDKF EQALSELGIP KPAGKTAVSV EEAVAIAEEI GYPVLVRPSY VLGGRAMEIV
YNRGELLHYM EHAVRVNPQH PVLVDRYITG KEVEVDAIAD GETVVIPGIM EHIERAGVHS
GDSIAVYPPQ TLSAEVIDKI ADYTIRLARG LHIVGLLNIQ FVVSGSDVYV LEVNPRSSRT
VPFLSKITGV PMANLATKAI LGTKLAEMGY ETGVCPVRPG VYVKVPVFSF AKLRNVDISL
GPEMKSTGEV IGKDVTFEKA LYKGLVASGI HIQPHGAVLL TVADKDKEEA VELARRFADI
GYQLLATNGT AETLKAAGIP VTVVNKIHSA SPNILDVIRQ GKAQVVINTL TKGKQPESDG
FRIRREAVEN GIPCLTSLDT ARAMLQVLES MTFSTTAMTE GLVRS
