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
//