ID A0A0D2AEH4_9EURO Unreviewed; 1164 AA.
AC A0A0D2AEH4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=PV07_11512 {ECO:0000313|EMBL:KIW23302.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23302.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23302.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23302.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-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}.
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DR EMBL; KN847046; KIW23302.1; -; Genomic_DNA.
DR RefSeq; XP_016243518.1; XM_016398956.1.
DR AlphaFoldDB; A0A0D2AEH4; -.
DR STRING; 569365.A0A0D2AEH4; -.
DR GeneID; 27350706; -.
DR VEuPathDB; FungiDB:PV07_11512; -.
DR HOGENOM; CLU_000513_1_3_1; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000054466; 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:UP000054466};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 217..409
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 754..950
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1018..1164
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1164 AA; 128488 MW; 21AF2134CD5ED761 CRC64;
MASTARALRQ ASGILLRDCA PVPRLSARPF STRAPSLAVR QHLVNSKTPS WQQVKRFTRS
TKRRALVQEA PRPEAYLESG AIEYGKNLVD VKKVIVIGSG GLSIGQAGEF DYSGSQALKA
LKEAGVKSIL INPNIATIQT DHKLADEVYY LPVTPEYVTY VIEREKPDGI LLTFGGQTGL
NLGVQMNKMG IFDRYGVKVL GTSIKTLETS EDRDLFAKAL NEINIPIAQS IAVGTVEEAL
DAAEKVGYPI IVRSAYALGG LGSGFANNPE ELSNLSSRSL SLSPQILVEK SLKGWKEVEY
EVVRDAEDNC ITVCNMENFD PLGIHTGDSI VVAPSQTLSD EEYHMLRTAA IKIVRHLGVV
GECNVQYALQ PDGLDYRVIE VNARLSRSSA LASKATGYPL AYTAAKIGLG HTLPELPNAV
TKTTTANFEP SLDYIVVKIP RWDLSKFQHV KRDIGSAMKS VGEVMAIGRT FEESFQKAIR
QVDPRYVGFQ GDKFDNLDDV LRNPTDRRWL AVGQAMIHEN YSVDKIHDLT KIDKWFLHKL
QNLKDTMTEI QEIGSLNGIK HELMLKAKKQ GFSDKQIAMY VKSTEGEVRV RRQKFGIRPW
VKKIDTLAAE FPADTNYLYT TYNASSHDVT FEDKGTIILG SGVYRIGSSV EFDWCAVNAT
LSLRSMGQKT VMINYNPETY STDFDTADKL YFEELSYERV MDIYELESAS GVVVSVGGQL
PQNIALRLQE EGKAHVLGTN PVDIDRAEDR HKFSQILDSI GVDQPAWKEL TSVADAESFA
DSVGYPVLVR PSYVLSGAAM SVIYTHEELK DKLESASAVS PDHPVVITKF IEGAQEIDVD
AVASKGELIL HAVSEHVEAA GVHSGDATLV LPPANLDENV MARVKEIAQK VAKAWNITGP
FNMQIIKADA PGEEPALKVI ECNLRASRSF PFVSKVLGTN FIDVATKALV GQNVPEPRDL
MAEKRDYLAT KVPQFSWTRL AGADPFLGVE MSSTGEIACF GKDLIEAYWA SLQSTMNFRM
PEPGEGILLG GSTELPELPK IVEYLQPLGY KFYAASQDVK DHLEKSGATI EVIEFPTTDK
NALRQVFQKY DIRGVFNLAK TRGKTLVDED YVMRRNAVDF GVPLFMEPKT ALLFAQCMNA
KLPRQEGIPP EVKSWSEFAG SKMM
//
