ID A0A2G7G2D0_9EURO Unreviewed; 2255 AA.
AC A0A2G7G2D0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Aspartate carbamoyltransferase {ECO:0000313|EMBL:PIG87017.1};
GN ORFNames=AARAC_010400 {ECO:0000313|EMBL:PIG87017.1}, BDV24DRAFT_5672
GN {ECO:0000313|EMBL:KAE8335612.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG87017.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG87017.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG87017.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAE8335612.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 117612 {ECO:0000313|EMBL:KAE8335612.1};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; ML737213; KAE8335612.1; -; Genomic_DNA.
DR EMBL; NEXV01000203; PIG87017.1; -; Genomic_DNA.
DR STRING; 656916.A0A2G7G2D0; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR Proteomes; UP000325558; 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; 3.20.20.140; 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; 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};
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:UP000231358};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIG87017.1}.
FT DOMAIN 604..796
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1139..1330
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1396..1545
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2255 AA; 248113 MW; E1B9C0B86ED27D26 CRC64;
MPHSAGHEEV ALPSSPLTGG AVSYNQINKE LQPLPSMDLT SGAVIPPASS RVRGGSGKLF
ALELEDGTVY QGYSFGAEKS VAGELVFQTG MVGYPESVTD PSYRGQILVV TFPLVGNYGV
PSRETMDELL KTLPKYFEST EIHIAALVVA TYAGEDYSHF LAESSLGQWL KEQGVPAMHG
VDTRALTKRI RQKGSMLGRM LLQKSDETLE EAPVDKDSWR SYFEETEWVD PNKKNLVNEV
SIREPRLFSP PENVALKHPS GRTVRVLCLD VGLKFNQLRC LLARGVEVLV VPWDYDFPTL
AGKDYDGLFV SNGPGDPATL TTTVNNLSKT LKEARTPVFG ICLGHQLIAR SVGAQTLKMK
FGNRGHNIPC TSMVTGKCHI TSQNHGYAVD STSLPEDWEE LFVNANDGSN EGIRHTSRPF
FSVQFHPEST PGPRDTEYLF DVFINSIKDT LTSPEAINNP VTFPGGTMEE NIKASPRVSV
KKVLILGSGG LSIGQAGEFD YSGSQAIKAL KEEGIYTILI NPNIATIQTS KGLADKVYFL
PVNADFVRKV IKHERPDAIY VTFGGQTALQ VGIQLKDEFE SLGVKVLGTP IDTIITTEDR
ELFARSMDSI NEKCAKSASA SNLEEALRVV EDIKFPVIVR AAYALGGLGS GFANNMEELK
DLCTKAFAAS PQVLIEKSMK GWKEIEYEVV RDARDNCITV CNMENFDPLG IHTGDSIVVA
PSQTLSDEDY NMLRTTAVNV IRHLGVVGEC NIQYALNPFS KEYCIIEVNA RLSRSSALAS
KATGYPLAFI AAKLGLGIPL NEIKNSVTKV TCACFEPSLD YCVVKIPRWD LKKFTRVSTQ
LGSSMKSVGE VMSIGRTFEE AIQKAIRSVD FHNLGFNETS ALMSIKGELQ TPSDQRLFAI
ANAMAAGYSV DDIWKLTQID KWFLSRLKGL SDFSKLMSTH NATTVPRPLI RQAKQLGFSD
RQLAKFLSSN ELAIRRMRVE AGIIPIVKQI DTVAAEFPSV TNYLYLTYNA SEHDVAFDDK
GIMVLGSGVY RIGSSVEFDW CSVRTIRTLR EQGYKTVMVN YNPETVSTDY DEADRLYFEN
INLETVLDIY QLESSSGVIM SMGGQTPNNI ALPLHRLNVR ILGTSPEMID GAENRYKFSR
MLDRIGVDQP AWKELTSIEE ATGFCDKVGY PVLVRPSYVL SGAAMNTVYS EHDLASYLNQ
AAEVSREHPV VITKYIENAK EIEMDAVALN GTMVGHFISE HVENAGVHSG DATLILPPQD
LDPETVRRIE EATRKIGNAL NVTGPYNIQF IAKDNDIKVI ECNVRASRSF PFVSKVMGVD
LIEMATKAML GVPFQEYPPV SVPKDYVGVK VPQFSFSRLS GADPVLGVEM ASTGEVASFG
RDKYEAYLKA LLSTGFRLPK RNVLFSIGSY KEKLEMLPSI RKLHQIGFNL FATSGTADFL
KENGVPVKYL EILPGQEDEL KSEYSLTQHL SNNLIDLYIN LPSSNRFRRP ANYMSKGYRT
RRMAVDYQTP LVTNVKNAKI LIEAIARHYD LAVQTIDYQT SHRTVTLPGL INIAAFVPGL
MTPGSKDFER VTKASIAAGF SMVRVMPVGI DASVTDARAL KVAQQNAQNA SFCDFNFSVV
ATSTNSEQIG QVTGDVGSLF IPFNHLSGNI SKVAAVTSHF GAWPSSKPII TDAKSTDLAS
VLLLASLHSR NIHVMSVSSK EDITLIALSK EKGLKVTCDV SVFSLFLSQE DYPECSFLPS
AEDQKALWEH LSTIDVFSIG SIPFQLAGEK ASPEVGIAET LPLLFTAVSD GRLTIQDIIA
RLYENPKKIF ELHDQVDCLV EVEVDRPYLF QNAHAWSPIS GKSVKGSVQR VTFQGKTSCL
DGEITPDAPK GTDMSAHRIV PASPSVKAMS PLVQARPEGI DGRLSVAGTP ARPSRRALDQ
APAVGELGPP LYPTVSQTSS PLHEMLSRST FRQKHVLSVG QFTRADLHLL FTVAQEMRLG
VQRQGVLDVL KGRVLCTLFY EPSTRTSASF DAAMQRLGGR TIAISTEHSS TKKGETLQDT
LRTLGCYGDA VVLRHPDPAS TEIAAKFSPV PVINGGNGSV EHPTQAFLDL FTIREELGTV
TGLTITFTGD LRYGRTVHSL IKLLQFYDVR VQLVAPKDLS LPEEVRQQVI ASGQLVVESE
ELTPEIVARS DVLYSTRVQK ERFADLEQYE RLKNSFVIDN ALLKHAKSHM VVMHPLPRNA
EIAEEVDFDQ RAAYFRQMRY GLYCRMALLA LILAP
//
