ID W5D791_WHEAT Unreviewed; 1172 AA.
AC W5D791;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDM83233.1, ECO:0000313|EnsemblPlants:TraesCS3B02G238600.1};
GN ORFNames=CFC21_041342 {ECO:0000313|EMBL:KAF7029647.1},
GN TRAES_3BF042100190CFD_c1 {ECO:0000313|EMBL:CDM83233.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EMBL:CDM83233.1};
RN [1] {ECO:0000313|EMBL:CDM83233.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25035497; DOI=10.1126/science.1249721;
RA Choulet F., Alberti A., Theil S., Glover N., Barbe V., Daron J.,
RA Pingault L., Sourdille P., Couloux A., Paux E., Leroy P., Mangenot S.,
RA Guilhot N., Le Gouis J., Balfourier F., Alaux M., Jamilloux V., Poulain J.,
RA Durand C., Bellec A., Gaspin C., Safar J., Dolezel J., Rogers J.,
RA Vandepoele K., Aury J.M., Mayer K., Berges H., Quesneville H., Wincker P.,
RA Feuillet C.;
RT "Structural and functional partitioning of bread wheat chromosome 3B.";
RL Science 345:1249721-1249721(2014).
RN [2] {ECO:0000313|EMBL:KAF7029647.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7029647.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3B02G238600.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3B02G238600.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [4] {ECO:0000313|EnsemblPlants:TraesCS3B02G238600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [5] {ECO:0000313|EMBL:KAF7029647.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7029647.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; HG670306; CDM83233.1; -; Genomic_DNA.
DR EMBL; CM022218; KAF7029647.1; -; Genomic_DNA.
DR SMR; W5D791; -.
DR STRING; 4565.W5D791; -.
DR PaxDb; 4565-Traes_3B_FE91A007E-1; -.
DR EnsemblPlants; TraesCS3B02G238600.1; TraesCS3B02G238600.1; TraesCS3B02G238600.
DR Gramene; TraesCAD_scaffold_100511_01G000100.1; TraesCAD_scaffold_100511_01G000100.1; TraesCAD_scaffold_100511_01G000100.
DR Gramene; TraesCLE_scaffold_001461_01G000300.1; TraesCLE_scaffold_001461_01G000300.1; TraesCLE_scaffold_001461_01G000300.
DR Gramene; TraesCS3B02G238600.1; TraesCS3B02G238600.1; TraesCS3B02G238600.
DR Gramene; TraesCS3B03G0614200.1; TraesCS3B03G0614200.1.CDS; TraesCS3B03G0614200.
DR Gramene; TraesKAR3B01G0255570.1; cds.TraesKAR3B01G0255570.1; TraesKAR3B01G0255570.
DR Gramene; TraesPAR_scaffold_016689_01G000300.1; TraesPAR_scaffold_016689_01G000300.1; TraesPAR_scaffold_016689_01G000300.
DR Gramene; TraesROB_scaffold_084987_01G000100.1; TraesROB_scaffold_084987_01G000100.1; TraesROB_scaffold_084987_01G000100.
DR Gramene; TraesWEE_scaffold_014758_01G000100.1; TraesWEE_scaffold_014758_01G000100.1; TraesWEE_scaffold_014758_01G000100.
DR HOGENOM; CLU_000513_1_0_1; -.
DR OMA; ENAAYYY; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000019116; Chromosome 3B.
DR Proteomes; UP000815260; Chromosome 3B.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR CDD; cd01424; MGS_CPS_II; 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 HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 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; IPR033937; MGS_CPS_CarB.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 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; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000019116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 203..399
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 761..954
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1021..1162
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 27..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 127566 MW; B5AB43A46D6BE701 CRC64;
MATSLSSHSQ LRACPSHAHR ATVLSRSLLP FPRRHHGSSR RGLSARSASS NGAAQDTAVT
VRHFAAEPTK GGKLSGVKKI MILGAGPIVI GQACEFDYSG TQACKALVEE GYEVVLVNSN
PATIMTDPDL AHRTYIGPMT PPLVEGIIAS ERPDALLPTM GGQTALNLAV SLAESGALDR
LGVRLIGASL PAIRAAEDRQ LFKQAMDRIG LKTPPSGIGT TLEECLAIAK DIGEFPLIVR
PAFTLGGTGG GIAYNRAEFE DICRSGLAAS HTQQVLVEKS LLGWKEYELE VMRDMADNVV
IICSIENIDP MGVHTGDSIT VAPAQTLTDK EYQRLRDHSV AIIREIGVEC GGSNVQFAVN
PTDGEVMVIE MNPRVSRSSA LASKATGFPI AKMAAKLSVG YTLDQIPNDI TKKTPASFEP
SIDYVVTKIP RFAFEKFPGS EPILTTQMKS VGESMALGRT FQESFQKAVR SLETGFAGWG
CAPIKELDWD WEKIKYSLRV PNPDRIHAVY AAFKKGMRVE DIHEISFIDK WFLTELKELV
DVEQFLVSKN LDQLSKDDFY QVKRRGFSDK QIAFATSSSE SDVRARRSAL GVTPTYKRVD
TCAAEFEANT PYMYSSYEYE CESAPTNRKK VLILGGGPNR IGQGIEFDYC CCHASFALRE
AGYETIMMNS NPETVSTDYD TSDRLYFEPL TVEDVTNVID LERPDGIIVQ YGGQTPLKLA
LPIQRHLEEK KLRSASGTGF VKIWGTSPDS IDAAEDRKRF NAILEELGIE QPKGGIARSE
SDALSIASEV GYPVVVRPSY VLGGRAMEIV YNDEKLIKYL ATAVQVDPER PVLVDKYLND
AIEIDIDALA DSVGNVVIGG IMEHIEQAGI HSGDSACSLP TRTVSTKCLD IIRSWTTKLA
KRLNVCGLMN CQYAITPTGE VYLLEANPRA SRTVPFVSKA IGHPLAKYAS LIMSGVTLPE
LGFTKEVIPK HVSVKEAVLP FEKFQGCDIL LGPEMRSTGE VMGIDYEFSG AFAKAQIAAG
QILPISGTVF VSLNDLTKRH LAEIGRGFRE LGFNIIATSG TAKVLQLEGI PVEPVLKIHE
GRPNARDMLK NGQIQVMVIT SSGDDLDSRD GLQLRRLALA YKVPIITTVD GARATMDAIK
SMKNKSIEIL ALQDYFQPAD APQKLPAAQA AP
//
