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Database: UniProt
Entry: A2QRW1_ASPNC
LinkDB: A2QRW1_ASPNC
Original site: A2QRW1_ASPNC 
ID   A2QRW1_ASPNC            Unreviewed;      2277 AA.
AC   A2QRW1;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   13-SEP-2023, entry version 104.
DE   SubName: Full=Contig An08c0170, genomic contig {ECO:0000313|EMBL:CAK39989.1};
DE            EC=2.1.3.2 {ECO:0000313|EMBL:CAK39989.1};
DE            EC=6.3.5.5 {ECO:0000313|EMBL:CAK39989.1};
GN   ORFNames=An08g07420 {ECO:0000313|EMBL:CAK39989.1};
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK39989.1, ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK39989.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC   {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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   -!- 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   -!- 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; AM270172; CAK39989.1; -; Genomic_DNA.
DR   MEROPS; C26.956; -.
DR   EnsemblFungi; CAK39989; CAK39989; An08g07420.
DR   HOGENOM; CLU_000513_2_1_1; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000006706; Chromosome 8R.
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:0046872; F:metal ion binding; IEA:InterPro.
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; 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_01209; CPSase_S_chain; 1.
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; IPR017926; GATASE.
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:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 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; 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; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAK39989.1};
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:UP000006706};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAK39989.1}.
FT   DOMAIN          606..798
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1141..1332
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1398..1547
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1890..1909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        344
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   2277 AA;  250330 MW;  8D9012BC94C4B789 CRC64;
     MPQSAGHEEA ALPSSPLSGG AVAYSQINKE LQPLPPMEAH TGAVIPPASA PYRGSNGRMV
     AVELEDGTVY QGYSFGAEKS ISGELVFQTG MVGYPESITD PSYRGQILVV TFPLVGNYGV
     PSRDTMDELL KTLPKYFEST QIHIAGLVVA TYAGEEYSHF LAQSSLGQWL KEQGVPAVHG
     VDTRALTKRI RQKGSMLGRL LLQKSETVSD ATVIPTEKDS WKPFFEQIEW VDPNKKNLVA
     EVSIKEPKLF SPPENVALKH PSGRPVRVLC LDVGLKFNQL RCLLARGVEV LVVPWDYDFP
     TLAGKDYDGL FVSNGPGDPA TLTTTVNNLS KTLKEARTPV FGICLGHQLI ARSVGAQTLK
     MKFGNRGHNI PCTSMLSGKC HITSQNHGYA VDSNSLPEGW EELFVNANDG SNEGIRHVSR
     PFFSVQFHPE STPGPRDTEY LFDVFINSIQ DTIASSEALQ KPVSFPGGVK EENIRIAPRV
     SVKKVLILGS GGLSIGQAGE FDYSGSQAIK ALKEEGIYTV LINPNIATIQ TSKGLADKVY
     FLPVNADFVR KVIKHERPDA IYCTFGGQTA LQVGIQLKDE FESLGVKVLG TPIDTIITTE
     DRELFARSMD SINEKCAKSA SASNLEEAMG VVESIGFPVI VRAAYALGGL GSGFADNMDE
     LRELCVKAFA ASPQVLIERS MKGWKEIEYE VVRDARDNCI TVCNMENFDP LGIHTGDSIV
     VAPSQTLSDE DYNMLRTTAV NVIRHLGVVG ECNIQYALNP FSKEYCIIEV NARLSRSSAL
     ASKATGYPLA FIAAKLGLGI PLNEIKNSVT KVTCACFEPS LDYCVVKIPR WDLKKFTRVS
     TQLGSSMKSV GEVMAIGRTF EEAIQKAIRS VDFHNLGFNE TNALMSIKGE LQTPSDQRLF
     AIANAMATGY SVDDIWKLTQ IDKWFLSRLK GLSDFSKLMT QYNATSVPRP LIRQAKQLGF
     SDRQLAKFLS SNELAVRRLR VESGIIPIVK QIDTVAAEFP SVTNYLYLTY NASEHDVNFE
     DKGIMVLGSG VYRIGSSVEF DWCSVRAIRT LREQGHKTVM VNYNPETVST DYDEADRLYF
     ENINLETVLD IYQLESSSGV IISMGGQTPN NIALPLHRLN VRILGTSPEM IDGAENRYKF
     SRMLDRIGVD QPAWKELTST EEATEFCNKV GYPVLVRPSY VLSGAAMNTV YSEHDLASYL
     NQAAEVSREH PVVITKYIEN AKEIEMDAVA RNGVMVGHFI SEHVENAGVH SGDATLILPP
     QDLDPETVRR IEEATRKIGN ALNVTGPYNI QFIAKDNDIK VIECNVRASR SFPFVSKVMG
     VDLIEMATKA MIGAPFAEYP PVSIPKDYVG VKVPQFSFSR LSGADPVLGV EMASTGEVAS
     FGRDKYEAYL KALISTGFRL PKRNVLFSIG SYKEKMEMLP SIRKLHQIGF NLFATSGTAD
     FLKENGVPVK YLEILPGEEE DIKSEYSLTQ HLANNLIDLY INLPSNNRFR RPANYMSKGY
     RTRRMAVDYQ TPLVTNVKNA KILIEAIARH FALNVQTIDY QTSHRTIILP GLINVAAFVP
     NLMVPGSPDF QLMTKASIAA GFSMVRVMPV GVDASVTDAR ALKIAQQNAE KSSFCDFNFS
     VVATTDNADQ IGQVTGDVGS LFIPFNHLSG NISKVATVTN HFGAWPSSKP IITDAKSTDL
     ASVLLLASLH SRNIHVMSVS SKEDISLIAL SKEKGLKVTC DVSVYSLFLT KDDFPECSSL
     PSVEDQKALW EHLSTIDVFS VGSIPYQVAG EKSSPVAGIA ETLPLLFTAV SEGRLTVEDI
     IARLYENPKK IFELHDQADS SVEIEVDRPY LFQAPQGAWS PFNGKNVRGA VQRVVFQGKT
     SCLDGEIISD ASTGTDMSTH RIVPASPSVK AMSPMVHARP ESSLDRRLSF SGTPLRPGRK
     LAEQAPAVGE LGPPLYTPVP QVSSSLLEML SRSTFRQKHV LSVNQFTRAD LHLLFTVAQE
     MRLGVQRQGV LDVLKGRVLC TLFYEPSTRT SASFDAAMQR LGGRTIAIST EHSSTKKGET
     LQDTVRTLGC YGDAVVLRHP DSSSAETAAK FSPVPIINGG NGSVEHPTQA FLDLFTIREE
     LGTVTGLTIT FTGDLRYGRT VHSLLKLLQF YDVRVQLVAP KDLSLPEEVR QQVIASGQLV
     VESEELTPEI VARSDVLYST RVQKERFSDL AQYERLKNSF VIDNALLKHA KSHMVVMHPL
     PRNAEISEEV DFDQRAAYFR QVSFSPDPLF EHDADVGLQM RYGLYCRMAL LALILAP
//
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