CPSM_LITCT
ID CPSM_LITCT Reviewed; 1496 AA.
AC Q91293;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Carbamoyl-phosphate synthase [ammonia], mitochondrial;
DE EC=6.3.4.16;
DE AltName: Full=Carbamoyl-phosphate synthetase I;
DE Short=CPSase I;
DE Flags: Precursor;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8163471; DOI=10.1016/s0021-9258(17)32635-2;
RA Helbing C.C., Atkinson B.G.;
RT "3,5,3'-Triiodothyronine-induced carbamyl-phosphate synthetase gene
RT expression is stabilized in the liver of Rana catesbeiana tadpoles during
RT heat shock.";
RL J. Biol. Chem. 269:11743-11750(1994).
CC -!- FUNCTION: Involved in the urea cycle of ureotelic animals where the
CC enzyme plays an important role in removing excess ammonia from the
CC cell. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000250|UniProtKB:P07756};
CC -!- ACTIVITY REGULATION: Requires N-acetyl-L-glutamate (NAG) as an
CC allosteric activator. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
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DR EMBL; U05193; AAA19016.1; -; mRNA.
DR PIR; I51170; I51170.
DR AlphaFoldDB; Q91293; -.
DR SMR; Q91293; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IEA:UniProtKB-EC.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-KW.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 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; 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; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
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 Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Repeat; Transit peptide; Urea cycle.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 34..1496
FT /note="Carbamoyl-phosphate synthase [ammonia],
FT mitochondrial"
FT /id="PRO_0000029900"
FT DOMAIN 215..401
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 548..740
FT /note="ATP-grasp 1"
FT DOMAIN 1090..1281
FT /note="ATP-grasp 2"
FT DOMAIN 1352..1496
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 34..214
FT /note="Anthranilate phosphoribosyltransferase homolog"
FT ACT_SITE 290
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1388
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250"
FT BINDING 1391
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250"
FT BINDING 1407
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250"
FT BINDING 1433
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250"
FT BINDING 1436
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250"
FT BINDING 1445
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1496 AA; 163767 MW; 2360BF05D21B059E CRC64;
MTRILSVFKT AKTGVLNAAA HRYRGFSKAG VRLMSVKAQT ANLVLEDGTK IKGYSFGHPA
SVAGEVIFNT GLGGYVEAVT DPSYHGQILT LTNPIIGNGG APDTKARDAY GLMKYIESEN
IQASGLLVLD YSHEYSHWGA VKSLSEWLHE EKVPALCGID TRMLAKKIRD NKGAVLGKIE
FEGQPVEFID PNKRNLIAEV STKETKVFGK GNPVRIVAVD CGVKHNIIRQ LVKRGAEVHL
VPWNHDFSQM EYDGLLITSG PGNPELAKPL IQNLKKVFQS DRPEPIFGIC KGNEIAALAA
GGKTYRLPMA NRGQNQPVMI TLNGQAFITA QNHAYAVDNN SLPAGWKPLF VNINDQSNEG
IMHETKPIFT SQFHPEANPG PVDTEFLFDV YMSLIKKGKG TTLTSVMPKP ALQSKRIDVA
KVLILGSGGL SIGQAGEFDY SGSQAVKAMK EENVKTVLMN PNIASVQTNE VGLKQADTVY
FLPITPQFVT EVIKAEKTDG IILGMGGQTA LNCGVELFKR GVLKEYGVRV LGTSVESIMF
TEDRQLFSDK LNEIKEPIAP SFAVESVKDA LEAADKIGYP VMIRSAYALG GLGSGLCPDK
ETLTDLATKA LAMTNQILVE RSVVGWKEIE YEVVRDAADN CVTVCNMENV DAMGVHTGDS
IVVAPCQTLS NEECQMLRAV SIKVVRHLGI VGECNIQFAL HPTSLEYVII EVNARLSRSS
ALASKATGYP LAFIAAKIAL GIPLPEIKNV VSGKTTACFE PSLDYMVTKI PRWDLDRFHG
ASGLIGSSMK SVGEVMAIGR TFEESFQKAL RMCHPSVDGF TSNLPMNKAW SSDVNLRKEM
AEPTSTRMYS MAKAIQSGIS LDEINKLTAI DKWFLYKMQG ILNMEKTLKG SRSESVPEET
LRRAKQIGFS DRYIGKCLGL SETQTRELRL NKNVKPWVKQ IDTLAAEYPA ITNYLYLTYN
GQEHDIKFDD HGMMVLGCGP YHIGSSVEFD WCAVSSIRTL RHVGKKTVVV NCNPETVSTD
FDECDKLYFE ELSQERIMDV FQLEQCDGCI ISVGGQIPNN LAVPLYKNGV KIMGTSPMQI
DRAEDRSIFS AVLDELQIAQ APWKAVNSLD DALQFTKTVG YPCLLRPSYV LSGSAMNVVY
GEEELKTFLA EATRVSQEHP VVITKFIEGA REVEMDAVGK EGRVISHAIS EHVEDAGVHS
GDATLMIPTQ SISQGAIEKV KIATKKIATA FAISGPFNVQ FLVRGNDVLV IECNLRASRS
FPFVSKTLGV DFIDVATKVM IGEKIDESSL PTLERPVIPA DYVGIKAPMF SWPRLRGADP
VLKCEMASTG EVACFGQNVY SAFLKAMIST GFKLPQKGIL IGIQHSFRPH FLGTAQTLKD
EGFKLYATEA TADWLNANDI TATPVAWPSQ EGQSGPSSIY KLIKEGNIDM VINLPNNNTK
YVRDNFAIRR TAVDTGTALL TNFQVVKMFA EAIKYSGDLD AKSLFHYRQF GGAKPS
