ID A0A1S9DD88_ASPOZ Unreviewed; 1175 AA.
AC A0A1S9DD88;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=OAory_01092600 {ECO:0000313|EMBL:OOO07057.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO07057.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO07057.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO07057.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) 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:OOO07057.1}.
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DR EMBL; MKZY01000007; OOO07057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DD88; -.
DR VEuPathDB; FungiDB:AO090011000630; -.
DR eggNOG; KOG0370; Eukaryota.
DR OMA; FPFNKFP; -.
DR Proteomes; UP000190312; 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:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd01423; MGS_CPS_I_III; 1.
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:UP000190312};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 225..417
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 762..958
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1026..1175
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1175 AA; 129304 MW; DFA80DF6C320783D CRC64;
MVLTTRCGQA TASLLRQRCL AESRRSTLAL RPFSSQTTAH SAASSLRLQQ KTPSPWRPQQ
LRSFSSAISR LASESTNAPS AESYLASGIV KPGRNLVDVK KVLVIGSGGL SIGQAGEFDY
SGSQALKALK EAGVESVLIN PNIATIQTDH KLADEVYYLP VTPEYVTYVI ERERPDAIFL
SFGGQTALNL GVQMNRMGIF ERYGVRVLGT SIKTLETSED RDLFAKALNE INIPIAESIA
VNTVDEALKA AEEVGYPIIV RSAYALGGLG SGFANNPEEL RNLASRSLTL APQILVEKSL
RGWKEVEYEV VRDADNNCIT VCNMENFDPL GIHTGDSIVV APSQTLSDEE YHMLRTAAIK
IVRHLGVVGE CNVQYALQPD GLDYRVIEVN ARLSRSSALA SKATGYPLAY TAAKIGLGHT
LPELPNAVTK TTTANFEPSL DYIVTKIPRW DLSKFQHVNR DIGSAMKSVG EVMAIGRTFE
ESFQKAIRQV DPRFVGFQGD KFENLDEVLQ NPTDRRWLAV GQAMLHENYS VDKVHELTKI
DKWFLYKLQN IVDCHNELKE IGSLFGIQKE TMLKAKKLGF SDKQISLLVG ASEDDVRARR
KSFGITPWVK KIDTLAAEFP ADTNYLYTTY NATSHDVTFD DHGIIILGSG VYRIGSSVEF
DWCAVNATLS LRNMGKKTVM INYNPETYST DFDTADKLYF EELSYERVMD IYELETASGV
VVSVGGQLPQ NIALRLQETG GANVLGTDPV DIDKAEDRHK FSSILDSIGV DQPAWKELTS
VADAERFAES VGYPVLVRPS YVLSGAAMNV IYSQDELKEK LLNASAVSPD HPVVITKFIE
GAQEIDVDAV ASNGKLLLHA VSEHVEPAGV HSGDATLVLP PAYLDESVMG RVKEIAEKVA
KAWNITGPFN MQIIKADQEG AQPELKVIEC NLRASRSFPF VSKVLGTNFI DTATKALVGR
DVPEPVDLMT EKRDYVATKV PQFSWTRLAG ADPFLGVEMS STGEIACFGK DLVEAYWASL
QSTMNFRVPE PGEGILLGGD IKNPALAKIV EYLQPLGYKF FAASASVKDH IESTAKESVS
VQVIEFPKKD KRALREVFEK YNIRGTFNLA KTRGKTLLDE DYVMRRNAVD FGVPLFMETK
TALLFAQAMS EKLPRAEGMP SEVRSWSEFA GGKLL
//
