ID A0A1G4MIL4_LACFM Unreviewed; 1121 AA.
AC A0A1G4MIL4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LAFE_0G17172G {ECO:0000313|EMBL:SCW03740.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW03740.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|EMBL:SCW03740.1, ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6772 {ECO:0000313|EMBL:SCW03740.1};
RA Devillers H.;
RL Submitted (MAR-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}.
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DR EMBL; LT598486; SCW03740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MIL4; -.
DR STRING; 4955.A0A1G4MIL4; -.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000190831; Chromosome g.
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:UP000190831};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 157..349
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 701..896
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 964..1121
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1121 AA; 123750 MW; 88A2D5588332F7FD CRC64;
MASVKSIYES TQPTTSAFNT KDYKPELVKG VKTVLVIGSG GLSIGQAGEF DYSGSQAIKA
LKEAGKRTIL INPNIATNQT SHSLADEIYY LPVTPEYITY IIERERPDAI LLTFGGQTAL
NCGVALDKMG VLEKYGIKVL GTPIKTLETS EDRDLFAQAL KQINIPIAES IACETIDQAL
DAAAKVGYPV IVRSAYALGG LGSGFANNEA EMKELTAQSL SLAPQILVEK SLKGWKEVEY
EVVRDRVDNC ITVCNMENFD PLGVHTGDSI VFAPSQTLSD EEFHMLRSAA IKIIRHLGVV
GECNVQYALQ PDGLDYRVIE VNARLSRSSA LASKATGYPL AYTAAKIALG YTLPELPNPV
TKTTVANFEP SLDYIVAKIP RWDLAKFQHV NRSIGSAMKS VGEVMAIGRN FEEAFQKAIR
QIDPTFIGFQ GSDEFGDDLD KVLAEPTDRR WLAVGQALIH EGYSVEKVHE LSKIDSWFLH
KCMNMVDMYK ELEAVNSLAE LDVDLITRAK KQGFSDKQIA ISINKNSSAN VHELEVRKLR
KSLGIVPFVK KIDTLAAEFP ANTNYLYTTY NATKSDIEFN DKGMLVLGSG VYRIGSSVEF
DWCAVNTARA LREEGKKTVM INYNPETVST DFDEVDRLYF EELSFERVMD IYELEHSEGC
VISVGGQLPQ NIALRLLEEG ANILGTSPID IDRAENRHKF SSILDKIGVD QPEWSELSSV
SDAKDFSRKV GYPVLIRPSY VLSGAAMSVV NSEHELESKL TNATDVSPDH PVVISKFIEG
AQEIDVDAVA YNGKVLAHAI SEHVENAGVH SGDATLILPP QNLSEDIKTR LKDIADKVAD
AWNITGPFNM QIIKDDRHAG TTLKVIECNI RASRSFPFVS KVLGVNFIDL AVKAFLGQKV
PEPVDLMAKG YPYVATKVPQ FSFTRLAGAD PFLGVEMAST GEVAAFGRDA LESYWTAIQS
TMNFHVPLPP SGILFGGDLS QEYLGQVARL VSPLGYKLFA TNQETKAYLE KYVHAGLQVA
IIEFPKNDKR KLRELFQEHD IKAVFNLAAK RAETLDDVDY VMRRNAIDFA IPLFNEPQTS
LLFARALSAK LAEKLRVLES TDVVVPTEVR TWHEWIGQRP M
//
