(data stored in SCRATCH3701 zone)

SWISSPROT: CARB_VIBVY

ID   CARB_VIBVY              Reviewed;        1077 AA.
AC   Q7MNU0;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 112.
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=VV0625;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
DR   EMBL; BA000037; BAC93389.1; -; Genomic_DNA.
DR   RefSeq; WP_011078652.1; NC_005139.1.
DR   SMR; Q7MNU0; -.
DR   STRING; 672.VV93_v1c05680; -.
DR   EnsemblBacteria; BAC93389; BAC93389; BAC93389.
DR   GeneID; 2623394; -.
DR   KEGG; vvy:VV0625; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 48855at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002675; Chromosome I.
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; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7MNU0.
DR   SWISS-2DPAGE; Q7MNU0.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome; Repeat.
FT   CHAIN           1..1077
FT                   /note="Carbamoyl-phosphate synthase large chain"
FT                   /id="PRO_0000145064"
FT   DOMAIN          133..328
FT                   /note="ATP-grasp 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          678..869
FT                   /note="ATP-grasp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          936..1077
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   NP_BIND         159..216
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   NP_BIND         704..761
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   REGION          1..403
FT                   /note="Carboxyphosphate synthetic domain"
FT   REGION          404..553
FT                   /note="Oligomerization domain"
FT   REGION          554..935
FT                   /note="Carbamoyl phosphate synthetic domain"
FT   REGION          936..1077
FT                   /note="Allosteric domain"
FT   METAL           285
FT                   /note="Magnesium or manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   METAL           299
FT                   /note="Magnesium or manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   METAL           299
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   METAL           301
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   METAL           828
FT                   /note="Magnesium or manganese 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   METAL           840
FT                   /note="Magnesium or manganese 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   METAL           840
FT                   /note="Magnesium or manganese 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   METAL           842
FT                   /note="Magnesium or manganese 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1077 AA;  117916 MW;  209D34114626B933 CRC64;
     MPKRTDIQSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPDM
     ADATYIEPIQ WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ALEKHGVLAE FGVEMIGATA
     DAIDKAEDRS RFDKAMKSIG LECPRADTAK TMEEAYKVLD MVGFPCIIRP SFTMGGTGGG
     IAYNKEEFEE ICRRGLDLSP TNELLIDESL IGWKEYEMEV VRDKADNCII VCSIENFDPM
     GIHTGDSITV APAQTLTDKE YQLMRNASLA VLREIGVETG GSNVQFGINP KDGRMVIIEM
     NPRVSRSSAL ASKATGFPIA KIAAKLAVGF TLDELQNDIT GGATPASFEP TIDYVVTKIP
     RFNFEKFAGA NDRLTTQMKS VGEVMAIGRN QQESLHKALR GLEVGATGFD EMVDLDSPDA
     LTKIRHELKE AGAERIWYIA DAFRAGMSVD GVFNLTNIDR WFLVQIEEIV KLEEQVKAGG
     FAGLTQDVLR QMKRKGFSDA RLSKLLGVAE SEIRRLRDQF DIHPVYKRVD TCAAEFSSDT
     AYMYSSYDDE CEANPTDKEK IMVLGGGPNR IGQGIEFDYC CVHASLALRE DGYETIMVNC
     NPETVSTDYD TSDRLYFEPV TLEDVLAIAR VEKPKGVIVQ YGGQTPLKLA RALEAAGVPI
     IGTSPDAIDR AEDRERFQQA VDRLGLLQPE NATVTTMEQA VEKSREIGFP LVVRPSYVLG
     GRAMEIVYDE QDLRRYFNEA VSVSNESPVL LDRFLDDAIE VDIDAICDGE RVVIGGIMEH
     IEQAGVHSGD SACSLPAYTL SQEIQDKMRE QVEKLAFELG VRGLMNTQFA VKDNEVYLIE
     VNPRAARTVP FVSKATGAPL AKIAARVMAG QSLESQGFTK EIIPPYYSVK EVVLPFNKFP
     GVDPLLGPEM RSTGEVMGVG ATFAEAYAKA ELGCGNVYPE GGRALLSVRE GDKQRVVDLA
     SKLLKLGYKL DATHGTAVIL GEAGINPRLV NKVHEGRPHI LDRIKNNEYT YIVNTAAGRQ
     AIEDSKVLRR GALAEKVNYT TTLNAAFATC MSHTADAKAS VTSVQELHAQ VQASLKA
//

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