ID A0A0C7MVA6_9SACH Unreviewed; 1118 AA.
AC A0A0C7MVA6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-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=LALA0_S09e04148g {ECO:0000313|EMBL:CEP63861.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP63861.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP63861.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP63861.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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; LN736368; CEP63861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7MVA6; -.
DR STRING; 1245769.A0A0C7MVA6; -.
DR HOGENOM; CLU_000513_1_3_1; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000054304; 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:UP000054304};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 154..346
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 698..893
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 961..1118
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1118 AA; 123759 MW; 2444F53615F19B8F CRC64;
MSSIYESSTP SISAFNTANY NPQLVKGVES VLVIGSGGLS IGQAGEFDYS GSQAIKALKE
ANKRTILINP NIATNQTSHS LADEIYYLPV TPEYITYIIE RERPDAILLT FGGQTALNCG
VALEKMGVLE KYNIKVLGTP IKTLETSEDR DLFAQALKEI NIPTAESFAC ETIDDALLAA
GRVGYPVIVR SAYALGGLGS GFANNEAEMK ELAAQALSLS PQILVEKSLK GWKEVEYEVV
RDRVGNCITV CNMENFDPLG VHTGDSIVFA PSQTLSDEEY HMLRTAAIKI IRHLGVIGEC
NVQYALQPDG LDYRVIEVNA RLSRSSALAS KATGYPLAYT AAKIALGYTL PELPNPVTKT
TVANFEPSLD YIVAKIPRWD LAKFQHVNRN VGSAMKSVGE VMAIGRNFEE AFQKAIRQID
PSFLGFQGSD EFGDDLDEVL ANPTDRRWLA IGQALIYEGY SVEKVHELSK VDAWFLHKCM
NMVEMYKELD AVNSLEALDK ELLTRAKKMG FSDKQIALSI NKNNENKVHE LDVRKYRKSF
GITPFVKKID TLAAEFPANT NYLYTTYNAT KSDVDFNDKG MLVLGSGVYR IGSSVEFDWC
AVNTARALRE SGKKTVMINY NPETVSTDFD EVDRLYFEEL SFERVMDIYD LENSEGCIIS
VGGQLPQNIA LKLQDNGAKI LGTDPVDIDR AENRHKFSSI LDSIGVDQPE WSELSSVEEA
EEFSNRVGYP VLIRPSYVLS GAAMSVVNSE DELLTKLTNA SDVSPDHPVV ISKFIEGAQE
IDVDAVAHKG EVLVHAISEH VENAGVHSGD ATLILPPQSL SQEIKDRLYE IAQKVAKAWK
ITGPYNMQII KDDRNHGTTL KVIECNIRAS RSFPFVSKVL GRNFIDAAVK AFIGEDVPKP
VNLMDEEYPY VATKVPQFSF TRLAGADPFL GVEMASTGEV ASFGKDALES YWTAMQSTMN
FHVPLPPSGV MFGGDLTKNQ LGEVAALVAG LGYKIYVTNE VTKEYLQKFV PADCDVMIIE
FPKNDKRKLR ELFQKYDIKA VFNLAARRAE SLEDVDYVMR RNAIDFALPL FNEPQTALLF
AKALTQKVGE KLKVLESSDV LVPPEVQTWH EWIGQRPM
//
