ID D8MAQ2_BLAHO Unreviewed; 1477 AA.
AC D8MAQ2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBK25141.2};
GN ORFNames=GSBLH_T00004775001 {ECO:0000313|EMBL:CBK25141.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK25141.2};
RN [1] {ECO:0000313|EMBL:CBK25141.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK25141.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN668690; CBK25141.2; -; Genomic_DNA.
DR RefSeq; XP_012899189.1; XM_013043735.1.
DR EnsemblProtists; CBK25141; CBK25141; GSBLH_T00004775001.
DR GeneID; 24921780; -.
DR InParanoid; D8MAQ2; -.
DR OMA; ENAAYYY; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000008312; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
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; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
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 HAMAP; MF_01209; CPSase_S_chain; 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; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
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 NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000008312};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 527..719
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1065..1256
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1327..1477
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 275
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1477 AA; 165107 MW; 19E919799D0415E0 CRC64;
MLESNACVDC MVVPNFGDTC IDRDIEKGKL ILADGTVFEG FSFGENVSRS GEVVFNTGMV
GYPESLTDPS YRGQILVFTF PMMGNYGIPG DELDEWGLPK YFESNEIHVA GVIVADYSWE
YSHWAARKSL SDWLKEHHIP ALYGIDTRML TKKIREHGVL LGKIEFAGQH VEIEDPNERN
LVAEVSIKEP RVFNKGLSPR VVAVDCGIKN NIIRCLCERK VQVTVVPFDY DLEAHRDEYD
GIFLSNGPGN PEMAQATIDH LKWAITTDIP IFGICLGNQL LALAAGARTY KMKFGNRAAN
VPCVDLTTGQ CFITSQNHGF AVDEKTLPPD WQPLFFNAND YSNEGIIHRT KKIFSSQFHP
EACAGPLDTR FLFDRFIANI KGAEQPLNTP LNTNFFRLQK FRKVLILGSG GLSIGQAGEF
DYSGSQAIKA MREEGLEVVL MNPNIATVQT SKNLADKVYF LPVTPSFVIR VIEKEKPDCM
LVSMGGQTAL NVGIKLFESG ELARHNVHVL GTPIQTVIDT EDRELFKERL DEINEKLALS
YPATSVEEAI EVAEKIGYPV LVRSAFALGG LGSGFAENRE ELVELVSRSF TCSDQLLIDK
DLRGWKEIEY EVVRDSYDNC VTVCNMENFD PLGIHTGDSI VVAPSQTLTN REYMLLRDTA
IKVVRHLGVI GECNIQYALN PDSEEYCIIE VNARLSRSSA LASKATGYPL AYVAAKLALG
NNLIQISNRV TSTTTACFEP SLDYCVVKVP RWDLKKFHRV SPLLGSCMKS VGEVMSIGRR
FEEALQKAVR MVNPLVQGFD LPSVEWSEEE LVRLLLHPDD RRIHALALAL ERNYSIDRIH
SITKIDNWFL AKLNNIHLAR KWLAGRRLEE LTVERMKVVK CLGFSDLQLA ALLSFPDALV
REARKALKVL PVVKQVDTLA AEFPATTNYL YMTYSGVEHD ITFHDHGVIV LGCGPYAIGS
SVEFDWAAVS CIRALKEAQK KTIVVNFNPE TVSTDYDESD RLYFEELSLE RILDIYEAEQ
SEGVIISVGG QIPNNLSLPL AENKVRIFGT SPSMIECAED RSKFSDLLDR LHIDQPEWVA
VTSESKAFEF AEKVSYPVLV RPSFVLSGAA MSVCMNENHL KACLGRAANI SSDYPVVVSK
FILGAKEIEF DAVADHGEII NYAISEHIEN AGVHSGDATL LLPSMKLYTE TERRIRAIAR
AIAKSLNITG PFNIQLLAKN NDVKVIECNL RASRTFPFIS KTFDFNFIEL ATRVMVGLPY
KRGNIVLRDL NYVGCKAPMF SFTRLSGADP TTGVEMASTG EVACYGESVS EAFLKSLLST
NFHFKFFDKN DTSARNFLIS IPENDFNQFT EGLEILQGMN VHFYATKGTF QRLAAFGIPA
ERLHRVYKSS ENVKENLALD YIRHQSIHLA IVVPSNNTDQ AITEGYKIRR MAVDFNIPLI
VNIKCAVEFV RAFEKYTLQG DDFLKIKCIQ EYYDGNK
//
