ID A0A196SIT5_BLAHN Unreviewed; 702 AA.
AC A0A196SIT5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carbamoyl-phosphate synthase small subunit {ECO:0000313|EMBL:OAO15859.1};
GN ORFNames=AV274_2415 {ECO:0000313|EMBL:OAO15859.1};
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO15859.1, ECO:0000313|Proteomes:UP000078348};
RN [1] {ECO:0000313|EMBL:OAO15859.1, ECO:0000313|Proteomes:UP000078348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAO15859.1}.
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; LXWW01000112; OAO15859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A196SIT5; -.
DR STRING; 478820.A0A196SIT5; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000078348; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; 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 CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
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; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 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; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000078348}.
FT DOMAIN 552..702
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 702 AA; 78235 MW; 63CC45BE6AFA2529 CRC64;
MTSSAESKVI ENFGDTCIDR DVEKGKLVLA DGTVFEGLSF GAPVSKSGEV VFNTGMVGYP
ESLTDPSYRG QILVFTFPMM GNYGVPGDEL DEWGLPKYFE SSDIHVAGVI VADYSWEYSH
WAAKKSLSEW LKVSLEHNIP ALYGIDTRML TKKIREKGSL LGKIEFVGQP VAIEDPNLRN
LVAEVSLKVP RVFNAGKSPR IVAVDCGIKN NIIRCLCQQE VQVTVVPFDY DLKAHAAEYD
GIFISNGPGN PEMAQATIEQ LKWAITTDIP IFGICLGNQL LALAAGGRTY KMKFGNRGAN
VPCVDLLSGQ CYITSQNHGF AVDEASLPAE WQPLFFNAND YSNEGIIHRT KKIFSSQFHP
EASAGPLDTR FLFKRFIDNV RGVETPLRAP LNTHFFRLQK FRKVLILGSG GLSIGQAGEF
DYSGSQAIKA LKEEGLEVVL MNPNIATVQT SKNLANKVYF LPVTTDKTFD FNFIELATRV
MVGLPYRRGN IVLKDLNYVG CKAPMFSFTR LSGADPTTGV EMASTGEVAC YGESVSEAFL
KAVLSTNFHF KFFTPEDQSV RNFLISIPED DFNQFREGIE ILKTMNIDFY ATKGTFARLQ
SCDIDPARLH RVYKSNEGNE DLAVDYIRRQ TVHLAIIVPN NNTDQAITEG YKIRRMAVDF
NVPLIVNIKC ALEFVRAFEK YTKQGPEFLK IKCMQEYYDG NK
//
