ID G8BY20_TETPH Unreviewed; 1112 AA.
AC G8BY20;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 Name=TPHA0I02970 {ECO:0000313|EMBL:CCE64798.1};
GN OrderedLocusNames=TPHA_0I02970 {ECO:0000313|EMBL:CCE64798.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE64798.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE64798.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE612864; CCE64798.1; -; Genomic_DNA.
DR RefSeq; XP_003687232.1; XM_003687184.1.
DR AlphaFoldDB; G8BY20; -.
DR STRING; 1071381.G8BY20; -.
DR GeneID; 11534532; -.
DR KEGG; tpf:TPHA_0I02970; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000005666; Chromosome 9.
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 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:UP000005666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 155..347
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 697..889
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 957..1112
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1112 AA; 122929 MW; C73538F7151547D8 CRC64;
MSIYKNTQPT VSIYNSECYN PQLLHDIKSV LIIGSGGLSI GQAGEFDYSG SQAIKAIKDS
NSNINIILIN PNIATNQTSH SLADRVYYLP VTPEYITYII EKERPDSILL TFGGQTGLNC
GISLKENGIL DKYNVKVLGT PIKTLVTSED RDLFAKALNE INIPIAESIA CDNIDDVIAS
ANKIGYPVII RSAYALGGLG SGFANNDTEL KNLASQSLAL APQVLVEKSM KGWKEIEYEV
VRDHVGNCIT VCNMENFDPL GVHTGDSIVF APSQTLSDEE FHMLRTAAIK IINHLGVIGE
CNVQYALQPD GLEYKVIEVN ARLSRSSALA SKATGYPLAY TAAKIALGYT LPELPNPITT
TTVANFEPAL DYIVAKIPKW DLSKFQYVNR DIGSAMKSVG EVMAIGRCYE EAFQKAIRQV
DPSLLGFQGS DEFEDLDEAL KTPTDRRLLA IGQALIVENY TVERVHELTK IDKWFLHKCS
NIVDIYKYLA QVKDITQLSY KLLLKAKKLG FSDKQIAKSI NIEEQLIDEL QIRELRKSKG
IIPFVKRIDT LAAEFPADTN YLYITYNATK SDIEFNDNGV LVLGSGVYRI GSSVEFDWCA
VNAAKSLREQ GKKTVMINYN PETVSTDFDE VDRLYFEELS LERVMDIYDL EHSEGCIISV
GGQLPQNIAL KLFENGYKTL GTSPVDIDNA ENRHKFSSIL DSIQVGQPEW SENSTLESAE
EFCNKVGYPV LIRPSYVLSG AAMSVVNSEE ELDKKLTLAS DISPDHPVVI SKFIEGAQEI
DVDAVAHNGS VLVHAISEHI ENAGVHSGDA SLVLPPQQIS SAIKTELLSI AKKVAKAWNI
TGPFNMQIIN DGIGPLKVIE CNIRASRSFP FVSKVLGVNF IDIAVKAFLS KHVPEPVDLM
SKEYNYVATK VPQFSFTRLA GADPFLGVEM ASTGEVASFG ANLIESYWTA IQSTSNFKVP
LPPSGILVGG DLTKNYIKNV VKTIDTLGFK IYVPNQSTYD YLTSEKEIQS EIIIAEIPAD
KSKLRKYFQQ LDIQTVFNLA SKKAEDTLDE NYIMRRSAID FAIPLFNEHE TSLLFAKCLQ
KKVDEKIKIL NSNDVVIPPE VHSWDEVLGF KA
//
