ID A0A2I1GHK2_9GLOM Unreviewed; 1200 AA.
AC A0A2I1GHK2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ammonium-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044318};
DE EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE AltName: Full=Arginine-specific carbamoyl phosphate synthetase, ammonia chain {ECO:0000256|ARBA:ARBA00044249};
DE AltName: Full=Glutamine-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044334};
GN ORFNames=RhiirA4_518931 {ECO:0000313|EMBL:PKY46112.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY46112.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY46112.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY46112.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) 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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000256|ARBA:ARBA00044031}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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:PKY46112.1}.
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DR EMBL; LLXI01000433; PKY46112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1GHK2; -.
DR VEuPathDB; FungiDB:FUN_020041; -.
DR VEuPathDB; FungiDB:GLOIN_2v1636357; -.
DR VEuPathDB; FungiDB:RhiirA1_417129; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 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; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 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; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 246..438
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 782..978
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1046..1200
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1174..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1200 AA; 132432 MW; 82722371EFC3D32D CRC64;
MYNNFIRSPS PVRRVSSILL SRVQTSIPRV SRGFHKTTTS TTRRILTPSI TTTPFQNSCV
TPSLGAFTSP YLRSFRPTTA RISYHFYNTS AVQHQEESAH KKVIDETRDL IFADVPKVDV
KKVLVVGSGG LSIGQAGEFD YSGSQAIKAL RESGVSTILV NPNIATIQTS HALADSVYFL
PVTVEYLTHI LERERPDGIL LTFGGQTGLN VGIKLEQMGV LKRLGIKVLG TPIRTLEVSE
DRALFADALK EIDIPVAQST AVSTIDDALA AADKIGYPII VRSAFALGGL GSGFANNPEE
LHSLAAKSLS LSPQILVEKS MKGWKEVEYE VVRDAANNCI TVCNMENFDP LGIHTGDSIV
VAPSQTLSDE EYHMLRTAAI KIIRHLGVVG ECNVQYALNP ESLEYKVIEV NARLSRSSAL
ASKATGYPLA FVAAKIALGH TLPELHNAVT KTTTACFEPS LDYIVTKIPR WDLSKFQHVN
REIGSSMKSV GEVMAIGRTF EESLQKAIRQ VDPSFKGFQS LPFPDLDKSL TVPTDRRLFA
VGHAMLEKNY TIDQIHNLTK IDKWFLYKLG NIVNVEHDIK HAEKLENVSK ELLQEAKKKG
FSDAQIAAML NTNEDQVRKV RKEYGITPFT KKIDTLAAEF PANTNYLYTT YNASTHDVKF
DDHGTMVLGS GVYRIGSSVE FDWCGVSAIR ALRDLGLKTL MVNYNPETVS TDFDECDRLY
FEELSYERVM DIYEQEAARG VIVSVGGQLP QNIALRMHQN EVNILGTSPV SIDKAEDRFK
FSQILDQIGV DQPEWKELSS AEEAEKFADK VGYPVLVRPS YVLSGAAMNV CHTREALHEN
LSEATSVSPL HPVVITKFIS PAAEIDVDAV AYKGKVLVHA VSEHVENAGV HSGDATLVLP
PRDINDHTMA RLKEIAQKVA KAFEITGPFN MQIIKKDNPD GESELKVIEC NLRASRSFPF
VSKVLGTNFI DVATKALCDK NVPEPVDLMA EKKDYQAVKV PQFSWTRLQG ADPFLGVEMA
STGEVACFGK DKYEAYWSAI QSTQNFRVPK IGGGILVGRD DLTNNDDFIT VASALSKDLG
HPLYTSSPKV TEYLAQNNIK ATTLALPEND KKALHQVFEN NNIDFVFNLA QLRASQTTDE
NYIARRSAVD FGIPLVNDSK CAVLFVEAVK RKRQESSSQA PGEHPSEVKS WSEFIGGKFC
//
