ID A0A0F4Z742_TALEM Unreviewed; 1174 AA.
AC A0A0F4Z742;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=T310_0046 {ECO:0000313|EMBL:KKA25916.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA25916.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA25916.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA25916.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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:KKA25916.1}.
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DR EMBL; LASV01000006; KKA25916.1; -; Genomic_DNA.
DR RefSeq; XP_013332528.1; XM_013477074.1.
DR AlphaFoldDB; A0A0F4Z742; -.
DR STRING; 1408163.A0A0F4Z742; -.
DR GeneID; 25312110; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IEA:UniProtKB-EC.
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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKA25916.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 225..417
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 762..959
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1027..1174
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1174 AA; 129340 MW; E8E8034E456DC682 CRC64;
MALSARCGQQ AAALLRQRCF AESRAPTLAL RSFSTHIPSR SAASCLRLQQ QIPSSWRSHQ
LRLFSSCLRR LASEAQTAPS TKAYLASGAI GRSPELVDVK KVLVIGSGGL SIGQAGEFDY
SGSQALKALK EAGVKSILIN PNIATIQTDH KLADEVYYLP ITPEYVTHVI EREQPDGIFL
SFGGQTALNL GVQMNRMGIF DRYGVKVLGT SIKTLEMSED RDLFAKALKE INIPIAESIA
CNTVDEALQA AESIGYPIIV RSAYALGGLG SGFAANREEL KNLASRSLSL APQILVEKSL
KGWKEVEYEV VRDASNNCIT VCNMENFDPL GIHTGDSIVV APSQTLSDEE YHMLRTAAIK
IVRHLGVVGE CNVQYALQPD GLDYRVIEVN ARLSRSSALA SKATGYPLAY TAAKIGLGHT
LPELPNAVTK TTTANFEPSL DYIVTKIPRW DLSKFQHVKR DIGSAMKSVG EVMAIGRTFE
ESFQKAIRQV DPRFVGFQGD HFEDLDEALR NPTDRRWLAI GQAMLHENYS VDRVHELTKI
DKWFLYKLQN IVDCHNELKE IGSLFGINQE MMLKAKKLGF SDKQIAMCVG STEDDVRARR
KSFGIRPWVK KIDTLAAEFP ADTNYLYTTY NATSHDVTFD DHGTIILGSG VYRIGSSVEF
DWCAVNATLT LRNMGKKTVM INYNPETYST DFDTADKLYF EELSYERVMD IYELENASGI
VVSVGGQLPQ NIALRLQEKG GAHVLGTDPV DIDKAEDRHK FSQILDSIGV DQPEWKELTS
VADAERFAET VGYPVLVRPS YVLSGAAMSV IYSPDELKEK LINASSVSPD HPVVITKFIE
GAQEIDVDAV ASGGKLLLHA VSEHVENAGV HSGDATLVLP PTSLNESDMA RLKEIAEKVA
KAWNITGPFN MQIIKADNPN GGEPLLKVIE CNLRASRSFP FVSKVLGTNF IDVATKALVG
RDVPEPVDLM ATKRDYVATK VPQFSWTRLA GADPFLGVEM ASTGEIACFG KDIIEAYWAS
LQSTMNFRVP EPGEGILLGG DYTGTLTKIV EYLQPLGYKF YAASPEVKAQ LESGVKGVSV
NVIEFPKEDK RALREIFQKY DIRGVFNLAK QRGKTLLDED YVMRRNAVDF GVPLFMEPKT
ALLFAQCMSE KLPRKEGIPP EVRSWSSFAG GKMM
//
