(data stored in ACNUC7421 zone)

SWISSPROT: C5B7N5_EDWI9

ID   C5B7N5_EDWI9            Unreviewed;      1073 AA.
AC   C5B7N5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 66.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210};
GN   OrderedLocusNames=NT01EI_0690 {ECO:0000313|EMBL:ACR67912.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67912.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00383240}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00710213};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611658};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00710244}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00710234}.
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:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}.
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DR   EMBL; CP001600; ACR67912.1; -; Genomic_DNA.
DR   RefSeq; WP_015870105.1; NC_012779.2.
DR   ProteinModelPortal; C5B7N5; -.
DR   STRING; 634503.NT01EI_0690; -.
DR   EnsemblBacteria; ACR67912; ACR67912; NT01EI_0690.
DR   GeneID; 7962024; -.
DR   KEGG; eic:NT01EI_0690; -.
DR   PATRIC; fig|634503.3.peg.621; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; POG091H01IP; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR033937; MGS_CPS_CarB.
DR   InterPro; IPR016185; PreATP-grasp_dom.
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.
PE   3: Inferred from homology;
DR   PRODOM; C5B7N5.
DR   SWISS-2DPAGE; C5B7N5.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710225};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710293};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710217};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710245, ECO:0000313|EMBL:ACR67912.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00710206};
KW   Manganese {ECO:0000256|SAAS:SAAS00511130};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00511109};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710218};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710196}.
FT   DOMAIN      133    328       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      679    870       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      404    553       Oligomerization domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      554    936       Carbamoyl phosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      937   1073       Allosteric domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01210}.
SQ   SEQUENCE   1073 AA;  117440 MW;  1800858D92DD3F20 CRC64;
     MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVVLVNSN PATIMTDPEM
     ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLAE FGVTMIGATA
     DAIDKAEDRR RFDQAMKKIG LDTARSGIAH SMEESLAVAE QVGFPCIIRP SFTMGGTGGG
     IAYNREEFEE ICARGLDLSP TNELLIDESL IGWKEYEMEV VRDKNDNCII VCAIENIDPM
     GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KSGRLIVIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP
     RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGASGFD PKVNLDDPQA
     LTKIRRELKD AGAERIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEQVADVG
     INGLTPDFLR QLKRKGFADA RLARLAGVAE SEIRKLRHKQ GLHPVYKRVD TCAAEFATDT
     AYLYSTYEEE CEANPTHDRP KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
     CNPETVSTDY DTSDRLYFEP VTLEDVLEIV AVERPQGVIV QYGGQTPLKL ARALEAAGVP
     VIGTSPDAID RAEDRERFQK AVNRLGLKQP ANATVTAIEQ AVEKGAQIGY PLVVRPSYVL
     GGRAMEIVYD ESDLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG ERVLIGGIME
     HIEQAGVHSG DSACSLPAYT LSAEIQDELR RQAEKLAMEL CVRGLMNVQF AVKDNQVYLI
     EVNPRAARTV PFVSKATGVP LAKVAARVMV GQTLAQQGMT EEVIPPYYSV KEVVLPFAKF
     PGVDPILGPE MRSTGEVMGV GRTFAEAFAK AMLGSLSQVK TPGRALLSVR EGDKHRVVDL
     AAKLLRQGFE LDATHGTAVV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIVNTTAGR
     QAIEDSKLIR RSALRYKVHY DTTLNGGFAT AMALNADPTE QVISVQEMHA RLK
//

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