ID Q4WM37_ASPFU Unreviewed; 2253 AA.
AC Q4WM37;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Bifunctional pyrimidine biosynthesis protein (PyrABCN), putative {ECO:0000313|EMBL:EAL88977.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EAL88977.1};
GN ORFNames=AFUA_6G11310 {ECO:0000313|EMBL:EAL88977.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88977.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL88977.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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=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:0000256|ARBA:ARBA00043687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
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 2nd section; belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00043998}.
CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily.
CC {ECO:0000256|ARBA:ARBA00043968}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
CC {ECO:0000256|ARBA:ARBA00043979}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00043984}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL88977.1}.
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DR EMBL; AAHF01000006; EAL88977.1; -; Genomic_DNA.
DR RefSeq; XP_751015.1; XM_745922.1.
DR SMR; Q4WM37; -.
DR STRING; 330879.Q4WM37; -.
DR MEROPS; C26.956; -.
DR EnsemblFungi; EAL88977; EAL88977; AFUA_6G11310.
DR GeneID; 3508320; -.
DR KEGG; afm:AFUA_6G11310; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_0_1; -.
DR InParanoid; Q4WM37; -.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAL88977.1};
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:UP000002530};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 607..799
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1142..1333
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1399..1578
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1864..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1889..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2253 AA; 247975 MW; B65C7B09C0B29694 CRC64;
MPQSAGNDEV ALPSSPLSGG AVSYNQINKE LQPLPSMDSG NGAVIPPASA RVRGSSGKMF
ALELEDGTIY QGYSFGAEKS VAGELVFQTG MVGYPESITD PSYRGQILVI TFPLVGNYGV
PSRETMDELL KTLPKYFEST EIHVAALVVA TYAGEDYSHF LAESSLGQWL KEQGVPAMHG
VDTRALTKRI REKGSMLGRM MLSKSEIADG VVEMTPGDKD SWRSSFEQVE WVDPNKKNLV
SEVSIREPRL FTPPENVALK HPSGRPVRVL CLDVGMKFNQ LRCLLARGVE VLVVPWDYDF
PKLAGKDYDG LFVSNGPGDP AMLSETVNNL SKTLKEARTP VFGICLGHQL IARSVGAQTL
KMKFGNRGHN IPCTSMLSGK CHITSQNHGY AVDSSTLPEG WEELFVNAND GSNEGIRHVS
RPFFSVQFHP ESTPGPRDTE YLFDVFINTI KDTLTSSDAL QKPVSFPGGT KAENIKTSPR
VSVKKVLILG SGGLSIGQAG EFDYSGSQAI KALKEEGIYT ILINPNIATI QTSKGLADKV
YFLPVNAEFV RKVIKHERPD AIYVTFGGQT ALQVGIQLKD EFESLGVKVL GTPIDTIITT
EDRELFARSM ESINEKCAKS ASASNLEEAL RVVEDIGFPV IVRAAYALGG LGSGFADNLD
QLKELCTKAF AVSPQVLIEK SMKGWKEIEY EVVRDCQDNC ITVCNMENFD PLGIHTGDSI
VVAPSQTLSD EDYNMLRTTA VNVIRHLGVV GECNIQYALN PFSKEYCIIE VNARLSRSSA
LASKATGYPL AFIAAKLGLG IPLNEIKNSV TKVTCACFEP SLDYCVVKIP RWDLKKFTRV
STQLGSSMKS VGEVMAIGRT FEEAIQKAIR SVDFHNLGFN ETNALMSIDQ ELQTPSDQRL
FAIANAMAAG YSVDDIWKLT RIDKWFLARL KRLSDFGKLM STYNATTVPR PLLREAKQLG
FSDRQLAKFL SSNELSIRRL RVEAGIIPIV KQIDTVAAEF PSVTNYLYLT YNASAHDVAF
DDNGILVLGS GVYRIGSSVE FDWCSVRTIR TLREQGLKTV MVNYNPETVS TDYDEADRLY
FENINLETVL DIYQLESSSG VVISMGGQTP NNIALPLHRL NVKILGTSPE MIDSAENRYK
FSRMLDRIGV DQPAWKELTS IEEAKGFCDK VGYPVLVRPS YVLSGAAMNT VYSEHDLATY
LNQAADVSRE HPVVITKYIE NAKEIEMDAV ARNGVMVGHF ISEHVENAGV HSGDATLILP
PQDLDPETVR RIEEATAKIG NALNVTGPFN IQFIAKDNDI KVIECNVRAS RSFPFVSKVM
GVDLIEMATK AMIGKPFAEY PPVTIPKNYV GVKVPQFSFS RLSGADPVLG VEMASTGEVA
SFGRDKYEAY LKALISTGFR LPKKNVLFSI GSYKEKMEML PSIKKLHQLG FNLFATSGTA
DFLKEHGVPV KYLEVLPGQE DDLKSEYSLT QHLANNLIDL YINLPSNNRF RRPANYMSKG
YRTRRMAVDY QTPLVTNVKN AKILIEAIAR HFALNVQTID YQTSHRTIIL PGLINITAFV
PGLVTPGSND FELVTKASIA AGFSMIRVMP VGVDASVTDA RALRVAQQNA QKASYCDFNF
SVVATSTNSE QVGQVTGEVG SLFIPFNHLS GNISKVTAVT NHFSVWPSSK PMITDAKSTD
LASILLLASL HSRNIHVMSV TSKEDINLIA LSKEKGLKVT CDVSIFCLFL SREDFPDCNF
LPSAEDQNAL WEHMSTIDVF SIGSIPFQLA GKQASPVSGI AESLPLLFTA VSEGRLTVED
IVSRLYENPK KIFELHDQAD TSVEIEVDRP YLFQSPYWSP FNGKSLRGAV QRVTFQGKTS
CLDGEVTRDA PKGTDMSGHR IVPASPSVKA MSPMVQARPE SSLDRRLSIS GTPGRSFKQR
PADSAANELG PPLYAPVQTS SSLHDLLSRS TFRQKHVISV NQFNRADLHL LFTVAQEMRL
GVQRQGVLDI LKGRVLTTLF YEPSTRTSAS FDAAMQRLGG RTIAISTEHS STKKGETLQD
TVRTLGCYGD AVVLRHPDPS SAETAAKFSP VPVINGGNGS VEHPTQAFLD LFTIREELGT
VTGLTITFTG DLRYGRTIHS LIKLLQFYHV RIQLVAPKDL SLPEEVRQTV VASGQLVLES
EELTPEIVAR SDVLYCTRVQ KERFADLEQY ERLKNSFIID NALMKHAKSH MVVMHPLPRN
AEIAEEVDFD QRAAYFRQVS CLSFSSLVCV ELC
//
