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Database: UniProt
Entry: C1A4I5
LinkDB: C1A4I5
Original site: C1A4I5 
ID   CARB_GEMAT              Reviewed;        1094 AA.
AC   C1A4I5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 58.
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=GAU_1968;
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC   Gemmatimonas.
OX   NCBI_TaxID=379066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505;
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y.,
RA   Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S.,
RA   Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that
RT   represents a novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009153; BAH39010.1; -; Genomic_DNA.
DR   RefSeq; WP_012683457.1; NC_012489.1.
DR   ProteinModelPortal; C1A4I5; -.
DR   SMR; C1A4I5; -.
DR   STRING; 379066.GAU_1968; -.
DR   EnsemblBacteria; BAH39010; BAH39010; GAU_1968.
DR   KEGG; gau:GAU_1968; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; GAUR379066:G1G2N-2019-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002209; 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_A; CPSase_L_chain_A; 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; 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;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1094       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000213876.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      679    870       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      937   1077       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     705    762       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    554       Oligomerization domain.
FT   REGION      555    936       Carbamoyl phosphate synthetic domain.
FT   REGION      937   1094       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       829    829       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       841    841       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       841    841       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       843    843       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1094 AA;  119125 MW;  5006DBC6AD3117EC CRC64;
     MPRRSDLHRI LVIGSGPIVI GQAAEFDYSG TQAIKALREE GYEVILVNSN PATIMTDPEF
     ADRTYVEPVT PEFVEKVIAK ERPDAVLPTM GGQTALNVAL ALHDSGVLAK YGCELIGANA
     RAIRVAEDRK LFGEAMEKIG LRCPTGRTVT SLEEALSAVE ETGFPAIIRP SFTLGGTGGG
     IAYNREEFET IVRRGLDLSP VHSVLIERSL LGWKEYELEV MRDCADNVVI VCSIENLDPM
     GVHTGDSITV APAMTLTDRE YQVMRDAAVA IIREIGVDAG GCNIQFAVNP TNGELIVIEM
     NPRVSRSSAL ASKATGFPIA RIGAKLAVGY TLDEVPNDIT KTTPASFEPV LDYVIVKCPR
     FAFEKFVSSD PGLTTQMKSV GESMAIGRTF KEAFQKALRA LETGRSGWTI AERLQDDRLT
     EGSKEELRGA LRRPTPERIF QLKRAMLLGM DTKELYEITA IDPWFLDQLR ELIDAEQWYE
     KLTGVDAVSM RRMKRLGFSD RQLGALRGQS ESDARAERWA LGVRPSYKMI DTCAGEFPSS
     TPYLYGNYDE ESEAATEGRK KVVILGSGPN RIGQGVEFDY CCVRAVLALR EQGYETIMVN
     SNPETVSTDF DISDKLYFEP LSLEDVLEIV HREQPEGVIV QLGGQTPLKL TRPLEAAGVK
     ILGTSPDAID AAEDRRRFEA IARELGIEQP ANGTATSVDE AVTIAQRIGF PVLVRPSYVL
     GGRAMEIVHD EVSLRDYFER AARVSEERPV LVDRFLEDAF EADVDALSDG TDVVIGAVME
     HIESAGIHSG DSACILPPYL IPAAAVAQMK EHTIAFAKRL GVVGLINVQY AYKDGQVYVI
     EVNPRASRTA PFVSKAIGVS LPSVAARLML GETLAEVGFT QEIIPPYISV KEAVFPFNKF
     REFDPVLGPE MRSTGEVMGI DDDFGAAFMK SQLAADNALP REGTVFFTVS DGDKPTAASL
     AGKFHSIGFS IMATSGTAAF FREQGIPVTS VLKVHEGRPH GVDKILNGEV QLLVNTPLGK
     HAQVDDEKLR QAAIANRLPY TTTLTAASAA FEAIAARRTR EPVVRSLQEW HEILRAPGAV
     ESATAGSTQP AGVA
//
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