GenomeNet

Database: UniProt
Entry: Q8YQL2
LinkDB: Q8YQL2
Original site: Q8YQL2 
ID   CARB_NOSS1              Reviewed;        1104 AA.
AC   Q8YQL2;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JAN-2019, entry version 111.
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=alr3809;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75508.1; -; Genomic_DNA.
DR   PIR; AB2282; AB2282.
DR   RefSeq; WP_010997950.1; NC_003272.1.
DR   ProteinModelPortal; Q8YQL2; -.
DR   SMR; Q8YQL2; -.
DR   STRING; 103690.alr3809; -.
DR   PRIDE; Q8YQL2; -.
DR   EnsemblBacteria; BAB75508; BAB75508; BAB75508.
DR   KEGG; ana:alr3809; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 48855at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002483; 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; 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   1104       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000144983.
FT   DOMAIN      133    329       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      703    900       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      967   1104       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     160    217       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     729    786       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT   REGION      404    552       Oligomerization domain.
FT   REGION      553    966       Carbamoyl phosphate synthetic domain.
FT   REGION      967   1104       Allosteric domain.
FT   METAL       286    286       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       300    300       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       300    300       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       302    302       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       854    854       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       871    871       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       871    871       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       873    873       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1104 AA;  121157 MW;  8B7E62C41AFCDDF9 CRC64;
     MPRRQDIQKI LLLGSGPIVI GQACEFDYSG TQACKALREE GYEVVLVNSN PATIMTDPET
     ADRTYIEPLT PELVEKVIAR ERPDALLPTM GGQTALNIAV ALAKNGVLDQ YNVELIGAKL
     PAIEKAEDRK LFNEAMDKIG VKVCPSGTAS SLDESKAIAR RIGTYPLIIR PAFTMGGTGG
     GIAYNQEEFE EMAQVGIDAS PVSQILIDQS LLGWKEYELE VMRDLADNVV IICSIENIDP
     MGIHTGDSIT VAPAQTLTDK EYQRLRDMAI KIIREIGVET GGSNIQFAVN PVNGDVVVIE
     MNPRVSRSSA LSSKATGFPI AKMAAKLAVG YTLDEIRNDI TKKTPASFEP TIDYVVTKVP
     RFAFEKFPGS EPVLTTQMKS VGEAMAIGRT FNESFQKALR SLETGRAGWG CDKAEKLPSG
     EQIRAQLRTP NPDRIFAVRH ALQLGMSPEE IYELTAIDPW FLDKMQQLLE VEKFLKRTPL
     KQLTREQMYA VKRDGYSDRQ IAFATKTTED EVRAYRKELG VTPVYKTVDT CAAEFEAFTP
     YYYSTYEEET EVIPASKPKV MILGGGPNRI GQGIEFDYCC CHAAYALKGA GYETIMVNSN
     PETVSTDYDT SDRLYFEPLT KEDVLNIIEA ENPVGIIVQF GGQTPLKLAL PLQDYLRQVG
     NGSLVIGNGN EETAITDDQL PITKIWGTSP DSIDSAEDRE RFEKILQKLN ISQPPNGIAR
     SYEDALIVAK RIGYPVVVRP SYVLGGRAME IVYSDTELER YMTFAVQVEP EHPILIDKFL
     ENAIEVDVDA IADHTGRVVI GGIMEHIEQA GIHSGDSACS LPSISLPPAV LNQIRTWTVQ
     LAQELSVVGL MNIQFAVIGA SSYSPQVYIL EANPRASRTV PFVSKATGVP LAKLASLIMS
     GKTLEELNFT QEVIPSHIAV KEAVLPFNKF PGTDTILGPE MRSTGEVMGI DSDFGRAFAK
     AELGAGERLP LTGTVFVSMS DRDKSAAVPV VREFIDLGFK VMATFGTRRV LLENGLNVEL
     VLKLHEGRPH VIDAIKNQKI QLIINTPSGE EAQTDARLIR RTGLAYKIPI ITTIAGAKAT
     VAAIRSMQNT TLDVKTIQEY CPNF
//
DBGET integrated database retrieval system