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Database: UniProt
Entry: O94313
LinkDB: O94313
Original site: O94313 
ID   CARB_SCHPO              Reviewed;        1160 AA.
AC   O94313;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   13-FEB-2019, entry version 133.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, ammonia chain;
GN   Name=arg4; ORFNames=SPBC215.08c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: In eukaryotes this enzyme is synthesized by two
CC       pathway-specific (arginine and pyrimidine) under separate control.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
DR   EMBL; CU329671; CAA22122.1; -; Genomic_DNA.
DR   PIR; T39898; T39898.
DR   RefSeq; NP_596685.1; NM_001022608.2.
DR   ProteinModelPortal; O94313; -.
DR   SMR; O94313; -.
DR   BioGrid; 277252; 4.
DR   DIP; DIP-59124N; -.
DR   IntAct; O94313; 1.
DR   STRING; 4896.SPBC215.08c.1; -.
DR   iPTMnet; O94313; -.
DR   MaxQB; O94313; -.
DR   PaxDb; O94313; -.
DR   PRIDE; O94313; -.
DR   EnsemblFungi; SPBC215.08c.1; SPBC215.08c.1:pep; SPBC215.08c.
DR   GeneID; 2540729; -.
DR   KEGG; spo:SPBC215.08c; -.
DR   EuPathDB; FungiDB:SPBC215.08c; -.
DR   PomBase; SPBC215.08c; arg4.
DR   HOGENOM; HOG000234583; -.
DR   InParanoid; O94313; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   PhylomeDB; O94313; -.
DR   Reactome; R-SPO-70635; Urea cycle.
DR   UniPathway; UPA00068; UER00171.
DR   PRO; PR:O94313; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005951; C:carbamoyl-phosphate synthase complex; ISO:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; EXP:PomBase.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   GO; GO:0000050; P:urea cycle; IC:PomBase.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1380; -; 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; 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; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 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; Cytoplasm; Ligase; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN         1   1160       Carbamoyl-phosphate synthase arginine-
FT                                specific large chain.
FT                                /FTId=PRO_0000145089.
FT   DOMAIN      212    404       ATP-grasp 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      748    946       ATP-grasp 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN     1014   1160       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     232    287       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     379    429       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       361    361       Manganese 1. {ECO:0000250}.
FT   METAL       375    375       Manganese 1. {ECO:0000250}.
FT   METAL       375    375       Manganese 2. {ECO:0000250}.
FT   METAL       377    377       Manganese 2. {ECO:0000250}.
FT   METAL       898    898       Manganese 3. {ECO:0000250}.
FT   METAL       917    917       Manganese 3. {ECO:0000250}.
SQ   SEQUENCE   1160 AA;  127480 MW;  883FBAC4A8E79BC7 CRC64;
     MALWATSMRR AIPGISKAFL GSNRVLETAG VSQLSKHLLP QWSGVPHRKI SASATNFNDK
     VKESNTPDAN AYIRSGHIKA AEHEKVKKVV VVGSGGLSIG QAGEFDYSGA QAIKALRESS
     VHTILINPNI ATIQSSHSLA DEIYFLPVTA EYLTHLIERE NPDGILLTFG GQTALNVGIQ
     LDDMGVFARN HVKVLGTPIS TLKTSEDRDL FAKALNEINI PIAESVAVST VDEALQAAEK
     VSYPVIIRSA YSLGGLGSGF ANNKEELQSM AAKSLSLTPQ ILVEKSLKGW KEVEYEVVRD
     AANNCITVCN MENFDPLGIH TGDSIVVAPS QTLSDEEYHM LRTAAIKIIR HLGVVGECNV
     QYALSPNSLE YRVIEVNARL SRSSALASKA TGYPLAYTAA KIALGHTLPE LPNAVTKTTT
     ANFEPSLDYV VTKIPRWDLS KFQYVNREIG SSMKSVGEVM AVGRTFEESL QKALRQVDPS
     FLGFMAMPFK DLDNALSVPT DRRFFAVVEA MLNQGYSIDK IHDLTKIDKW FLSKLANMAK
     VYKELEEIGS LYGLNKEIML RAKKTGFSDL QISKLVGASE LDVRARRKRL DVHPWVKKID
     TLAAEFPAHT NYLYTSYNAS SHDIDFNEHG TMVLGSGVYR IGSSVEFDWC GVSCARTLRK
     LGHSTIMVNY NPETVSTDFD ECERLYFEEL SYERVMDIYE METASGIVVS VGGQLPQNIA
     LKLQETGAKV LGTDPLMIDS AEDRHKFSQI LDKIGVDQPA WKELTSVAEA SKFANAVGYP
     VLVRPSYVLS GAAMSVIRDE SSLKDKLENA SAVSPDHPVV ITKFIEGARE LDVDAVASKG
     KLLVHAVSEH VENAGVHSGD ATIALPPYSL SEDILSRCKE IAEKVCKAFQ ITGPYNMQII
     LAQNPDKPDT PDLKVIECNL RASRSFPFVS KTLGVNFIDV ATRSIIDQEV PAARDLMAVH
     RDYVCVKVPQ FSWTRLAGAD PYLGVEMSST GEVACFGKDV KEAYWAALQS TQNFKIPLPG
     QGILLGGDRP ELAGIAADLS KLGYKLYVAN KDAAKLLQPT SAEVVEFPVK DKRALRAIFE
     KYNIRSVFNL ASARGKNVLD QDYVMRRNAV DFNVTLINDV NCAKLFVESL KEKLPSVLSE
     KKEMPSEVKR WSEWIGSHDL
//
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