CARB_SCHPO
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 03-AUG-2022, entry version 145.
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; Schizosaccharomycetaceae;
OC 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA 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; carbamoyl
CC 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 the
CC 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 pathway-
CC specific (arginine and pyrimidine) under separate control.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22122.1; -; Genomic_DNA.
DR PIR; T39898; T39898.
DR RefSeq; NP_596685.1; NM_001022608.2.
DR AlphaFoldDB; O94313; -.
DR SMR; O94313; -.
DR BioGRID; 277252; 7.
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 PomBase; SPBC215.08c; arg4.
DR VEuPathDB; FungiDB:SPBC215.08c; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR InParanoid; O94313; -.
DR OMA; IEPAGIH; -.
DR PhylomeDB; O94313; -.
DR Reactome; R-SPO-500753; Pyrimidine biosynthesis.
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:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; EXP:PomBase.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IC:PomBase.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
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; IPR011607; MGS-like_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; Cytoplasm;
KW Ligase; Manganese; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1160
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000145089"
FT DOMAIN 212..404
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 748..946
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1014..1160
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT BINDING 232..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 379..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 898
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 917
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="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
