(data stored in SCRATCH zone)

SWISSPROT: C5B7N4_EDWI9

ID   C5B7N4_EDWI9            Unreviewed;       385 AA.
AC   C5B7N4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 60.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209};
GN   Name=carA {ECO:0000256|HAMAP-Rule:MF_01209};
GN   OrderedLocusNames=NT01EI_0689 {ECO:0000313|EMBL:ACR67911.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67911.1, 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_01209}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-Rule:MF_01209}.
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_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01209}.
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DR   EMBL; CP001600; ACR67911.1; -; Genomic_DNA.
DR   RefSeq; WP_015870104.1; NC_012779.2.
DR   ProteinModelPortal; C5B7N4; -.
DR   STRING; 634503.NT01EI_0689; -.
DR   EnsemblBacteria; ACR67911; ACR67911; NT01EI_0689.
DR   GeneID; 7962023; -.
DR   KEGG; eic:NT01EI_0689; -.
DR   PATRIC; fig|634503.3.peg.620; -.
DR   eggNOG; ENOG4105C1M; Bacteria.
DR   eggNOG; COG0505; LUCA.
DR   HOGENOM; HOG000038087; -.
DR   KO; K01956; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; POG091H01NP; -.
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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B7N4.
DR   SWISS-2DPAGE; C5B7N4.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01209, ECO:0000313|EMBL:ACR67911.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN      196    383       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   REGION        1    195       CPSase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01209}.
FT   ACT_SITE    272    272       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01209}.
FT   ACT_SITE    356    356       {ECO:0000256|HAMAP-Rule:MF_01209}.
FT   ACT_SITE    358    358       {ECO:0000256|HAMAP-Rule:MF_01209}.
SQ   SEQUENCE   385 AA;  41771 MW;  319B317E552A6680 CRC64;
     MIKSALLVLE DGTQFHGRSI GADGSAVGEV VFNTSMTGYQ EILTDPSYSR QIVTLTYPHI
     GNVGTNAADE ESSTVHAQGL IVRDLPPIAS NFRCQETLPD YLRRHRVVAI ADIDTRKLTR
     LLREKGAMNG CIVTAENGSE PDAALALEKA RAFPGLKGMD LAKEVTTKEA YRWCQGSWTL
     SGGLPAPRDD AELPYHVVAY DFGVKRNILR MLVDRGCRLT VVPAQTPAQD VLALDPDGIF
     LSNGPGDPAP CDYAIEAIAT FLRGEIPLFG ICLGHQLLAL ASGAQTVKMK FGHHGGNHPV
     KDLEGDRVMI TAQNHGFAVD EATLPTTLRA THKSLFDGSL QGIHRTDRPA FSFQGHPEAS
     PGPHDAAPLF DHFMTLIENY RRTAK
//

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