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Database: UniProt
Entry: C5C687
LinkDB: C5C687
Original site: C5C687 
ID   CARB_BEUC1              Reviewed;        1109 AA.
AC   C5C687;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 62.
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};
GN   OrderedLocusNames=Bcav_2038;
OS   Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC   Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae;
OC   Beutenbergia.
OX   NCBI_TaxID=471853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432;
RX   PubMed=21304633; DOI=10.4056/sigs.1162;
RA   Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA   Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M.,
RA   Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Hauser L.,
RA   Chang Y.J., Jefferies C.C., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT   0122).";
RL   Stand. Genomic Sci. 1:21-28(2009).
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;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000255|HAMAP-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
CC       the 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}.
DR   EMBL; CP001618; ACQ80293.1; -; Genomic_DNA.
DR   RefSeq; WP_015882533.1; NC_012669.1.
DR   ProteinModelPortal; C5C687; -.
DR   SMR; C5C687; -.
DR   STRING; 471853.Bcav_2038; -.
DR   PRIDE; C5C687; -.
DR   EnsemblBacteria; ACQ80293; ACQ80293; Bcav_2038.
DR   KEGG; bcv:Bcav_2038; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; BCAV471853:G1GET-2064-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000007962; 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;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1109       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000213872.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      678    876       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      957   1102       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     704    768       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    550       Oligomerization domain.
FT   REGION      551    956       Carbamoyl phosphate synthetic domain.
FT   REGION      957   1109       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       835    835       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       847    847       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       847    847       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       849    849       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1109 AA;  118454 MW;  89CDEE1E812A0F5E CRC64;
     MPRRTDLTSV LVIGSGPIVI GQAAEFDYSG TQACRVLREE GLRVILVNSN PATIMTDPEF
     ADATYVEPIT PEVVASIIAK ERPDALLPTL GGQTALNTAI ALHEAGVLAE YDVELIGANI
     EAIHLAEDRD QFKGVVERCG AESARSHIAH TIEEVLEAAR DLGYPLVVRP SFTMGGLGSG
     IAYDEADLRR IAGAGLHYSP TTEVLLEESI LGWKEYELEL MRDRNDNVVV VCSIENVDPV
     GVHTGDSITV APALTLTDRE YQRLRDVGIA VIREVGVDTG GCNIQFAVHP DTGRVVVIEM
     NPRVSRSSAL ASKATGFPIA KIAARLAVGY TLDEIPNDIT GSTPASFEPT LDYVVVKVPR
     FAFEKFPAAD PLLTTTMKSV GEAMALGRNF TEALQKAMRS IDKAGSTFHW RGQAPDPERT
     AALVDAARTP TEGRLVQVQQ AIRGGATLEE LFEATAIDPW FLDQLFLLEE VAGRLAAVDA
     LDAGVLALAK RHGFSDAQVA EIRDLGEATV REIRHAYGLR PVYKTVDTCA AEFEARTPYH
     YSSYDAETEV QPRDRPAVLI LGSGPNRIGQ GIEFDYSCVH AALALKGEYE TVMVNCNPET
     VSTDYDTADR LYFEPLTFED VLEVYHAELA VGPVAGIIVQ LGGQTPLSLA TRLADAGLPI
     WGTPPEAIDA AEDRGVFGEV LVAAGLPAPA FGTATSLAQA RAVADRIGYP VLVRPSYVLG
     GRGMEIVYDV EQLTDYVRRA TPTDGPADAP VFASPVLIDR FLDEAIEIDV DALYDGHELF
     LGGVMEHIEE AGIHSGDSAC VLPPVTLSRR EIERIRTSTE AIARGVGVRG LLNVQFALSS
     DVLYVLEANP RASRTVPFVA KATGVPLAKA ASLLMAGATI ADLRASGHLP AVDGTYAHPS
     SPVAVKEAVL PFKRFRTRAG TVVDTVLGPE MRSTGEVMGY DVDVPAAFAK SQAAAYGGLP
     TSGRVFVSVA DRDKRSIVFP VARLVELGFE ILATTGTADV LRRYGIDSRV VRKASDGRGP
     DGELTVVDLI TAGEIDMVVN TPNGQGARAD GYDIRTATTA ADKPIVTTTQ QFAAAVLGIE
     AIRRGPFAVA SLQEHDAARA ARETEGVHA
//
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