ID A0A1A9VK89_GLOAU Unreviewed; 1924 AA.
AC A0A1A9VK89;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|RuleBase:RU004395};
DE EC=4.6.1.12 {ECO:0000256|RuleBase:RU004395};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT039685-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT039685-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT039685-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-
CC erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000200,
CC ECO:0000256|RuleBase:RU004395};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 4/6. {ECO:0000256|ARBA:ARBA00004709}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789}.
CC -!- SIMILARITY: Belongs to the IspF family.
CC {ECO:0000256|RuleBase:RU004395}.
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DR STRING; 7395.A0A1A9VK89; -.
DR EnsemblMetazoa; GAUT039685-RA; GAUT039685-PA; GAUT039685.
DR VEuPathDB; VectorBase:GAUT039685; -.
DR OrthoDB; 3642067at2759; -.
DR UniPathway; UPA00056; UER00095.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000078200; Unassembled WGS sequence.
DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-EC.
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:0070567; F:cytidylyltransferase activity; IEA:InterPro.
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:0006520; P:amino acid metabolic process; IEA:UniProt.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR CDD; cd00554; MECDP_synthase; 1.
DR CDD; cd01424; MGS_CPS_II; 1.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1330.50; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; 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; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR HAMAP; MF_00107; IspF; 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; IPR034683; IspD/TarI.
DR InterPro; IPR003526; MECDP_synthase.
DR InterPro; IPR020555; MECDP_synthase_CS.
DR InterPro; IPR036571; MECDP_synthase_sf.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR033937; MGS_CPS_CarB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR00151; ispF; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF02142; MGS; 1.
DR Pfam; PF02542; YgbB; 1.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00081; GDHRDH.
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; SSF69765; IpsF-like; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS01350; ISPF; 1.
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};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229,
KW ECO:0000256|RuleBase:RU004395}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU004395};
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 719..915
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1271..1462
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1525..1670
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1924 AA; 212741 MW; CDE07E9E4C9EA885 CRC64;
MELLYNHYLS EKSAVHSFQR VTLESRKKET SSQATWMTRG VDTKLLSPIY GGESRQSSVK
LGLESLQKIN PDFVVIHDAC RPFVSNVLID NLAQSMINDQ YTGVVPAIEV EDTMSLVGNN
FVESTISRGK LRAIQTPQIF NFKELLSCHQ SDKEFTDDSS LMVEHKKHVA IIKGEKSNFK
LTTKEDINMA KLLFEEPKFR VGTGYDIHKF IKVQNGAESF IKICGVKIEH NMAIEAHSDG
DVAIHAIVDA ILGALGCGDI GEHFPPSSSE WKDCNSSHFL DFAAKKAKEK GYSVSNLDIT
IVCEEPKISP YKVEMKKFIS KALEIENYVY ASYNFYGLSA TAPSLQITPP GVIFETTTGA
PKNTAVNAPS AKSAGHGILP NIASNAAPII TIVIIGPPMP SNISMNLAKE KEMGKLEGKV
ALITGASGKI GSAVAKRFIR EGACVILISR SLDNLKPLYN EIEELEEFKE GSVKLIQLDL
LDFENVKILT NMIESLKLSE SGALDILVAC TGISGKLNPI HDCEIEELQN VMNTNFTANW
YLLKNLDPML KKSNAGRVIF MTSEVTLSPS SYPYWMPYAA KTVIVIMPKR TDIESILVIG
AGPIVIGQAC EFDYSGTQSC KVLKSQGYKV ILVNSNPATI MTDPEFSDAT YIEPVLPEII
EKIIIKEMPD AILPTMGGQT ALNCAIKLAD DGVLDKYNVE LIGVNREAIK KAEDRELFRQ
SMDRIGLKYP KSIIIKNQEQ IKKALDYVGL PAIIRSSFTL GGAGSGIAYN KEEFFNIAES
ALKISPINEV QIDESIIGWK EYEMEVIRDC KDNCIIVCSI ENIDPMGVHT GDSITVAPAL
TLRDVEYQQM RNASIAVLRE IDVSAGGANV QFAVNPKEDG SLVVIEMNPR VSRSSALASK
ATGYPIAKVV TKLAIGYSLD EIRNDCAPII PAAFEPVIDY IVTKIPRFEF EKFKGTNCEL
STSMKSVGEV MSIGRTFNES LQKAFRSLET DLTGLDEVFP ENIDIDHVKS QLAKLLPNRL
LIAADAMRHG ISIEEINSIT GYDLWFLQNI QQIILAEQKI KENGLPETAY EMLELKKMGF
SDARLAKLSN KKVEQIEEIR KKFGINPVYK RVDTCAAEFE SSTAYMYGCY EGDVENKTEC
EANISDRKKV VILGSGPNRI GQGIEFDYAC VHAASAAKEM RYETIMINCN PETVSTDYDT
ADRLYFAPLI AEDVLEILNK EQENGTLVGV IVQIGGQTPL KLAKILNEKG FNILGTSFDS
IDLAEDRMRF KNLALQLNLK QPENSICHSV EEALTNAEKV GFPLVVRPSY VLGGQSMSIR
HDTQSFKEYV LNQTKIFEHG SLLLDKFLVN AVEVDVDAVC DGKKVFIAAV MEHIEEAGIH
SGDSTCSIPT NTLSDEVIKE IELQTERIAL ALKVKGLINI QFAVQESDVY ILEVNLRASR
TLPFISKVIN IPIAKLATQV ILGKNLNQEN KPFNHFAVKA AVFPFTRFAG VDTLLGPEMK
STGEVMGIDL SFEAALAKVH MAAGYKLPTE GTALVSVKDD DKEYILPVVR MLKELSFEIY
ATKGTALYLN NNGIAAKAVN KVREGRPHIV DMLKDGKINL VINTSKGVKS ASDSKDIRRT
AILQNIAYST TASGSKALVL AIQYTPCTEP SDWDSNSSCS SDYSCFLEGG SLLMDLEIPL
TKNEEKLIDE FCKEMKKVEE ENNKGSALRL IQYITNKYLG KGIRLNSCYG DRYRTVTNLI
FEEIIDVINN EGLCPNSKAH ALRGQDVSYS NEDQDDDNTN EVLEDGNLDI IRSTIRDLLL
KGGKVERGLF DGGELGHVTS DFDYVNDLFA ECKEIENDLK NVAYESIVNK NEQAQKDKLE
LKVKIDNECF CIKYPQDSTV EVAKILSNEK NKGLNLRVGI LQIGKSIVRV ESYNGKRNCL
STSF
//
