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Database: UniProt
Entry: H2QHM0_PANTR
LinkDB: H2QHM0_PANTR
Original site: H2QHM0_PANTR 
ID   H2QHM0_PANTR            Unreviewed;      2225 AA.
AC   H2QHM0; A0A2J8NKU4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=CAD protein {ECO:0000256|ARBA:ARBA00017075};
DE            EC=2.1.3.2 {ECO:0000256|ARBA:ARBA00013008};
DE            EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
GN   Name=CAD {ECO:0000313|EMBL:JAA02963.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000020200.3,
GN   ECO:0000313|VGNC:VGNC:58047};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000020200.3, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000020200.3, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA02963.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02963.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA34588.1}, Skin {ECO:0000313|EMBL:JAA28063.1}, and
RC   Smooth vascular {ECO:0000313|EMBL:JAA17301.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000020200.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC         Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000462};
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         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001363};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004880}.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC       hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008454}.
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DR   EMBL; AACZ04002054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01008375; JAA02963.1; -; mRNA.
DR   EMBL; GABF01004844; JAA17301.1; -; mRNA.
DR   EMBL; GABD01005037; JAA28063.1; -; mRNA.
DR   EMBL; GABE01010151; JAA34588.1; -; mRNA.
DR   RefSeq; XP_001155357.1; XM_001155357.3.
DR   SMR; H2QHM0; -.
DR   STRING; 9598.ENSPTRP00000086335; -.
DR   MEROPS; C26.952; -.
DR   PaxDb; 9598-ENSPTRP00000020200; -.
DR   Ensembl; ENSPTRT00000021897.4; ENSPTRP00000020200.3; ENSPTRG00000011756.6.
DR   GeneID; 470338; -.
DR   KEGG; ptr:470338; -.
DR   CTD; 790; -.
DR   VGNC; VGNC:58047; CAD.
DR   eggNOG; KOG0370; Eukaryota.
DR   GeneTree; ENSGT00940000157241; -.
DR   HOGENOM; CLU_000513_2_1_1; -.
DR   OrthoDB; 309at2759; -.
DR   TreeFam; TF105604; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002277; Chromosome 2A.
DR   Bgee; ENSPTRG00000011756; Expressed in fibroblast and 21 other cell types or tissues.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01316; CAD_DHOase; 1.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   CDD; cd01423; MGS_CPS_I_III; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
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; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
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   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          519..711
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1052..1243
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1308..1462
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1811..1899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1850..1877
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   2225 AA;  243012 MW;  E591A7AEA219552C CRC64;
     MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
     GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA TRTLHEWLQQ HGIPGLQGVD
     TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF LDPNARPLVP EVSIKTPRVF NTGGAPRILA
     LDCGLKYNQI RCLCQRGAEV TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL
     SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE
     TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF DIFLETVKEA
     TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
     KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT
     ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ
     AQAAAERLGY PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI
     EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ TAIKVTQHLG
     IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN
     SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL
     RMVDENCVGF DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM
     KRIIAHAQLL EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
     KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
     QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP
     NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT
     VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
     ASDGVVAAIA ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN
     LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV GLMTGSGVVG
     VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG
     SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
     LEQLAEKNFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
     GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV
     CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG SAAGLKLYLN
     ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL MVAQLTQRSV HICHVARKEE
     ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL ERLGPGKGEV RPELGSRQDV EALWENMAVI
     DCFASDHAPH TLEEKCGSRP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
     HLPPQEDTYV EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL
     VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH LPPRIHRASD
     PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS PQNLGTPGLL HPQTSPLLHS
     LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
     AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR
     PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
     LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA
     CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
     VLGRF
//
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