ID N1QDK3_SPHMS Unreviewed; 1879 AA.
AC N1QDK3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Aspartate carbamoyltransferase {ECO:0000313|EMBL:EMF09525.1};
GN ORFNames=SEPMUDRAFT_166200 {ECO:0000313|EMBL:EMF09525.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF09525.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF09525.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF09525.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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 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}.
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DR EMBL; KB456269; EMF09525.1; -; Genomic_DNA.
DR RefSeq; XP_016757646.1; XM_016908208.1.
DR STRING; 692275.N1QDK3; -.
DR GeneID; 27905345; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_1_1; -.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000016931; Unassembled WGS sequence.
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; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; 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; 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 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; 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};
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:UP000016931};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMF09525.1}.
FT DOMAIN 608..800
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1145..1336
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1402..1565
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 346
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1879 AA; 207209 MW; 60B40E59BF9025C4 CRC64;
MAEQLERFEA GESTGMALEV QDGDKTVRFC EGRSFGAHRS VAGELVFQTG MVGYPESITD
PSYRGQILVI TFPLVGNYGV PPRDALDPIL GDLPAHFEAS EIHVAGLVVA SYCGEDYSHH
LASSSLGAWL KEQNVPAICG VDTRALTKKI REKGSMLGRL LMQTGTRREL NGHASPTTGA
MTPSGTAPPT PAANLHEVNS ALTPRGADGR NGTNGYFSKS KEVAVYEEIE FYNPNSRNLV
ADVSTSKPKI YSTPASVTSL RHPSGRPVRV LCVDVGLKYN QLRCLVKRGV EVEVVPWDYD
FPGLAGKEYD GLFISNGPGD PAMMAATVKN IQQTMEEARV PIFGICLGHQ LLARAAGAST
LKMKFGNRGH NIPCTNLLSG KCYITSQNHG YAVDANSLPN GWSELFVNAN DESNEGIRHV
SRPYFSVQFH PESTPGPRDT EFLFDVFIST IQNVIKDSSF MQRPVVFPGG DIEENRALHP
RPDVKKVLVL GSGGLSIGQA GEFDYSGSQA IKALKEEGIY TILINPNIAT IQTSKGLADK
VYFLPVNAEF VRKVIKHERP DAIYCTFGGQ TALSVGIQLK DEFESLGVKV LGTPIDTIIT
TEDRELFARS MDSIGEPCAK SKSANNLQEA LDAVEEIGYP VIVRAAYALG GLGSGFASNK
EELVDLCHKA FAASPQILVE RSMKGWKEIE YEVVRDCNDN CITVCNMENF DPLGIHTGDS
IVVAPSQTLS DEDYNMLRTT AVRVIRHLGV VGECNIQYAL NPDSREFCII EVNARLSRSS
ALASKATGYP LAFVAAKLGL NIPLNEIKNS VTKKTVACFE PSLDYVVVKI PRWDLKKFTR
VSTLLGSSMK SVGEVMAIGR TFEEAVQKAI RSVDPSNLGF HNTPALMDIN IDTELQTPSD
QRMFALANAL HSGYTVDKIW ELTKIDKWFL RKLKSLNDFG KLMTGYGVDS IPAPLFRKAK
EMGFSDKQLS LFWDSNEGNV RRARLANNLM PFVKQIDTVA AEFPAYTNYL YTTYHGTEHD
IEFKDRGIMV LGSGVYRIGS SVEFDWCSVR AIRTLRTAGF KTVMVNFNPE TVSTDFDEAD
RLYFENITLE TILDIYQLES ASGVILSMGG QAPNNIALPL YRANVKVLGT SPEMIDTAEN
RYKFSRMLDR LGVDQPEWKE LTSIDEARSF CNRVTYPVLV RPSYVLSGAA MNTVYSEHDL
KNYLAQAVEV SKEHPVVITK YIENAKEIEM DAVAHNGTMI GHFVSEHVEN AGVHSGDATL
ILPPQDLDPE TVRKIEDATR KIGDALNVTG PYNIQFIAKD NEIKVIECNV RASRSFPFVS
KVTGLDMIEL ATKAMAGLPF QAYPPVTLRP DYVAVKVPQF SFSRLAGADP VMGVEMASTG
EVACFGRTKY EAYMKGLIST GFKLPKKNVL LSIGSYKDKV EMLPSIEKLY KLGFKLFATA
GTADYLEEHG ISVQFLEALG SDDQREEYSL THALANNLID LYINLPSANK YRRPANYMSK
GYRTRRMAVD FQTPLVTNVK IAKILIEGLS RNYDFNISSV DYQTFAEQTL VPSTVQQPAP
TEPLSELIKR SPFKGKDIIS VKQLTKEELH LLFTVAAEMR LGVERDGCLD ILKGRVLCTM
FFEPSTRTSC SFDAAMKRLG GQTIVVNEAH SSTKKGESLA DTIRTLDQYG DAIVLRHPDN
ESAEIAAKYS DRPIINAGNG SREHPTQALL DLFTMREELG TVNGLTITFT GDLKYGRTVH
SLCEVLKHYN VKIQLAAPAA LALPSKVRAN LEARGQLGIV SEKLTPEIIA DTDVLYCTRV
QHERFESEAA YEEALEEGGF TVNAKTLRDA KKNMIVMHPL PRNAELAVDV DDDPRAAYFR
QMKYGMFVRM ALLALVMAP
//
