ID Q5B0D1_EMENI Unreviewed; 1173 AA.
AC Q5B0D1; C8V347;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 125.
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=ANIA_05999 {ECO:0000313|EMBL:CBF70389.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF70389.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
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DR EMBL; BN001301; CBF70389.1; -; Genomic_DNA.
DR RefSeq; XP_663603.1; XM_658511.1.
DR AlphaFoldDB; Q5B0D1; -.
DR STRING; 227321.Q5B0D1; -.
DR EnsemblFungi; CBF70389; CBF70389; ANIA_05999.
DR GeneID; 2871108; -.
DR KEGG; ani:AN5999.2; -.
DR VEuPathDB; FungiDB:AN5999; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR InParanoid; Q5B0D1; -.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:EnsemblFungi.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0097308; P:cellular response to farnesol; IEP:AspGD.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
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:UP000000560};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 223..415
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 760..956
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1024..1173
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1173 AA; 128867 MW; 815D7F43C757D3C3 CRC64;
MVLAARCGQA TSSLLRQRCL AETRRSALAL RSFTSPSTTR STASALRLQQ KTPSPWRSQQ
LRNFSSALCR LAAESSSVGD SLFSSGIVNP GANLVDVKKV LVIGSGGLSI GQAGEFDYSG
SQALKALKEA GVQSVLINPN IATIQTDHKL ADEVYYLPVT PEYVTYVIER ERPDGIFLSF
GGQTALNLGV QMNRMGTFER YGVRVLGTSI KTLETSEDRD LFAKALNEIN IPIAESIAVG
TVDEALKAAD EVGYPIIVRS AYALGGLGSG FANNPEELKN LASRSLTLSP QILVEKSLRG
WKEVEYEVVR DASNNCITVC NMENFDPLGI HTGDSIVVAP SQTLSDEEYH MLRTAAIKIV
RHLGVVGECN VQYALQPDGL DYRVIEVNAR LSRSSALASK ATGYPLAYTA AKIGLGHTLP
ELPNAVTKTT TANFEPSLDY IVTKIPRWDL SKFQHVNRDI GSAMKSVGEV MAIGRTFEES
FQKAIRQVDP RFVGFQGDKF ENLDEVLKNP TDRRWLAVGQ AMLHENYSVD KVHELTKIDK
WFLYKLQNIV DNHNELKEIG SLFGVNKELM LKSKKLGFSD KQIAQLVGAS EDDVRARRKG
FGIRPWVKKI DTLAAEFPAD TNYLYTTYNA TSHDVTFDDH GTIILGSGVY RIGSSVEFDW
CAVNATLSLR NMGKKTVMIN YNPETYSTDF DTADKLYFEE LSYERVMDIY ELESASGVVV
SVGGQLPQNI ALRLQETGGA NVLGTNPKDI DNAEDRHKFS QILDSIGVDQ PAWKELTSVA
EAERFAEAVG YPVLVRPSYV LSGAAMSVIH SQDELKEKLL NASAVSPDHP VVITKFIEGA
QEIDVDAVAS NGKLLLHAIS EHVEPAGVHS GDATLVLPPA SLEKPVMSRV KEIAEKVAKA
WNITGPFNMQ IIKADQEGAE PQLKVIECNL RASRSFPFVS KVLGTNFIDV ATKALVGRDV
PEPVDLMEVK RDYLATKVPQ FSWTRLAGAD PFLGVEMAST GEIACFGKDV VEAYWASLQS
TMNFRVPEPG EGILLGGDIT NPALAQIVDL LHPLGFKFFA ASPEVKAHIE SATKEHTPVQ
VIEFPKKDKR ALREVFQKYD IRGCFNLAKT RGKTLLDEDY VMRRNAVDFG VPLFMETKTA
QLFAQAMNQK LPRPEGIPSE VRTWSNFVGG KLL
//
