ID A0A2H3EDU0_ARMGA Unreviewed; 2275 AA.
AC A0A2H3EDU0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carbamoyl-phosphate synth {ECO:0000313|EMBL:PBK98603.1};
GN ORFNames=ARMGADRAFT_1008993 {ECO:0000313|EMBL:PBK98603.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK98603.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293648; PBK98603.1; -; Genomic_DNA.
DR STRING; 47427.A0A2H3EDU0; -.
DR InParanoid; A0A2H3EDU0; -.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000217790; 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:UP000217790};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2275
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013722759"
FT DOMAIN 634..826
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1169..1360
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1425..1606
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 379
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2275 AA; 249350 MW; E9085EA77D01D54D CRC64;
MWQASTSSGP HPFFFFFFFL SPRTRTPGSN PGGEEDDDEN RRQSILYHLS LTMSTTRPAL
SRTPSSLFPT PLASAPYAQN NKSTLSGDNA VLELGDGSAF RGISFGAEGT SVAGECVFQT
GMVGYTESLT DPSYEGQILI LTYPLIGNYG VPKRPSAASD LPAEFESSRI HVAAIVVGNY
SKDFSHFLAE SSLSDWLKEN GVPAIYGVDT RALTKKIREK GSMLGKILAR RPEMPLGRKF
SLNPVSSRAS SPYTTASWRE DYFDIPFQDP NQINLVAEVS ITEPRLYSPT IAPHLHPSGR
PIRVLAVDVG MKYNQIRCFI NRGVELLVVP WDYDFLHESE PYDGIFISNG PGDPSLLSST
IARLSEVMKN ADKPIFGICL GHQLLALAAG AKTSKMKYGN RGHNIPCTDM LSGRCYITSQ
NHGFQVDTPT LPAGWKELFR NANDGSNEGI YCEDKPFFSV QFHPESTPGP RDTEFLFDVF
IKNIVDCATT ISLPGGKKED NDKRVPRANV TKVIILGSGG LSIGQAGEFD YSGSQAIKAL
KEEGIYTIMV NPNIATIATS KGLADKVYFL PVTPEFVRKI IKYEKPDGIY VTFGGQTALN
VGIKLKDEFA ELGVQVLGTP IDTIITTEDR QLFASAMAEI GEKCAESCTA VNQEEAINAA
RTIGFPVIVR AAYALGGLGS GFAQDEAQLK ALCSKAFATS PQVLVEKSMK GWKEIEYEVV
RDCRDNCITV CNMENFDPLG IHTGDSIVVA PSQTLSDSDY NMLRTTAINV IRHLGVVGEC
NIQYALNPSS QEYCIIEVNA RLSRSSALAS KATGYPLAFI AAKLGLGIPL NEIKNSVTKV
TSACFEPSLD YVVVKIPRWD LKKFNRVSRL LSSSMKSVGE VMSIGRTFEE TIQKAIRAID
DQFSGFAKND FVEDIDEELV NPTDKRIFAI STAFHRGYSI DKIWQMTNID KWFLAKLKYI
YEMEVLLGGY GVSTLTPDIL RQAKQLGFSD RQLATCVGST ELAVRTLRKE QGIAPFVKQI
DTVAAEFPAF TNYLYTTYNA VEHDISFNDR GVMVLGSGVY RIGSSVEFDW CAVRAIRTLR
DEGLPTVMVN YNPETVSTDY DEADRLYFEN ISLETILDIY DAEQSRGVIL SMGGQTPNNI
ALPLYRENVK IYGTSPEMID TAENRFKFSR LLDEIGVDQP LWKELTSFDE AYAFCEKVGY
PVLVRPSYVL SGAAMNVVST GDDLQNYLTQ ATAVSRDHPV VITKYIEQAK EIEMDAVAKD
GKMVMHYISE HVENAGVHSG DATLIHPPQD LDPQTVRQIA EATAKIGNAL NVTGPFNIQF
IAKNNEIKVI ECNLRAARSF PFVSKVTGID AIEMATKVML DLSVESYPDS GLPPDYVGVK
VPQFSFSRLS GADPVLGVEM ASTGEVACFG HDKYEAYLKA LISTGIVPPK KNILFSIGSY
REKLELLPSV QKLSAAGYNI FATSGTADFL TEHNVSCKYL ETLGEDNRDK QKSEYSLTQH
LANNLIDMYI NLPSKNHYRR PASYTSKGYH TRRMAVDFAV PLITNVKNAK MLAEALVRKL
PLDVSTVDSK SSHQTHTFPG LVSIATFVPS LVEPGSKDLE EATEASLSAG FTTAIVIPIG
HSTRITDRAS LDVAKANLKG SAHCNFALTL AASAQNVQGL DDELQAEAKA LFIPFNVDHV
TISLSAVAAH FTSWTSDKPI VTNAKGSDLA SVLLLASLHN RSVHVTDVLT SDDLLLISLS
KAKHLKVTCD VSVYSLFFNR SQFPKSTCLP TTEDQKAIWS KLETIDAFSV GATPYLLATE
EGETTSPWSG MEETLPLLLT AVADGRLTLE DIRLRLHDNP VLIFGLPEQS NTTVEVVVGR
KAPFGKRETC WSPVEKGFVT GAIHRVIVHG QTNFLDGALT SSPNGKDISS ATITHPSVAA
LVSPALKAAE PASLGAIATF AMGLPMAPPG HPTIQGPPAW NITSHLLPHP SFHRRHILSV
KQFTHRDMYD LFSLAHEMRL QVERNGTLDV LKGKVLCTAF YEPSTRTSSS FDAAMKRCGG
QVVQISADNS SVMKGETLPD TIRTLACYGD AIVIRHPDVG SAQLAAKFSP VPIINAGDGI
GEHPTQALLD VYTIRSELGT VNGRTITLLG DLKNGRTVHS LVTLLSLYSV QLNFVSPPSL
AMPANVVSAA RKAGIPVTIC ESLEDVLHDT DVLYVTRVQK ERFETEAEWM QVKDAYRVDH
AVLSRAKEDM IVMHPLPRVN EIDPEVDFDS RRAVYFRQMR YGLFIRMALL MSVLL
//
