ID D7KEN0_ARALL Unreviewed; 1183 AA.
AC D7KEN0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFH67096.1};
GN ORFNames=ARALYDRAFT_473200 {ECO:0000313|EMBL:EFH67096.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348713; EFH67096.1; -; Genomic_DNA.
DR RefSeq; XP_002890837.1; XM_002890791.1.
DR AlphaFoldDB; D7KEN0; -.
DR STRING; 81972.D7KEN0; -.
DR EnsemblPlants; fgenesh2_kg.1__3154__AT1G29900.1; fgenesh2_kg.1__3154__AT1G29900.1; fgenesh2_kg.1__3154__AT1G29900.1.
DR GeneID; 9326899; -.
DR Gramene; fgenesh2_kg.1__3154__AT1G29900.1; fgenesh2_kg.1__3154__AT1G29900.1; fgenesh2_kg.1__3154__AT1G29900.1.
DR KEGG; aly:9326899; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_0_1; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:EnsemblPlants.
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:0016036; P:cellular response to phosphate starvation; IEA:EnsemblPlants.
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:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 220..416
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 778..971
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1038..1179
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1183 AA; 129537 MW; 17CC99B8B37A3CAA CRC64;
MSNHCLELSS NCSSIFASSK SNPRFSPSST FFSRSAINYR AKSKLASSSS SFSSFLPCLN
RKSSLTRALK PVSELADTTT KPYSREIVGK RTDLKKIMIL GAGPIVIGQA CEFDYSGTQA
CKALREEGYE VILINSNPAT IMTDPETANR TYIAPMTPEL VEQVIEKERP DALLPTMGGQ
TALNLAVALA ESGALEKYGV ELIGAKLGAI KKAEDRELFK EAMKNIGLKT PPSGIGNTLD
ECFDIAERIG EFPLIIRPAF TLGGTGGGIA YNKEEFESIC KAGLAASVTS QVLVEKSLLG
WKEYELEVMR DLADNVVIIC SIENIDPMGV HTGDSITVAP AQTLTDREYQ RLRDYSIAII
REIGVECGGS NVQFAVNPVD GEVMIIEMNP RVSRSSALAS KATGFPIAKM AAKLSVGYTL
DQIPNDITRK TPASFEPSID YVVTKIPRFA FEKFPGSQPL LTTQMKSVGE SMALGRTFQE
SFQKALRSLE CGFSGWGCAK IKELDWDWDQ LKYSLRVPNP DRIHAIYAAM KKGMKIDEIY
ELSMVDKWFL TQLKELVDVE QYLMSGPLSE ITKEDLYEVK KRGFSDKQIS FATKTTEEEV
RTKRISLGVV PSYKRVDTCA AEFEAHTPYM YSSYDFECES APNSKKKVLI LGGGPNRIGQ
GIEFDYCCCH TSFALQDAGY ETIMLNSNPE TVSTDYDTSD RLYFEPLTIE DVLNVIDLEK
PDGIIVQFGG QTPLKLALPI KHYLDKHMPM SLSGAGPVRI WGTSPDSIDA AEDRERFNAI
LDELKIEQPK GGIAKSEADA LAIAKEVGYP VVVRPSYVLG GRAMEIVYDD SRLITYLENA
VEVDPERPVL VDKYLSDAIE IDVDTLTDSY GNVVIGGIME HIEQAGVHSG DSACMLPTQT
IPSSCLQTIR QWTTKLAKKL NVCGLMNCQY AITTSGDVFL LEANPRASRT VPFVSKAIGH
PLAKYAALVM SGKSLKDLNF EKEVIPKHVS VKEAVFPFEK FQGCDVILGP EMRSTGEVMS
ISSEFSSAFA MAQIAAGQKL PLTGTVFLSL NDMTKTHLEK IAVSFLELGF KIVATSGTAH
FLELKGIPVE RVLKLHEGRP HAADMVANGQ IHLMLITSSG DALDQKDGRQ LRQMALAYKV
PVITTVAGAL ATAEGIKSLK SSAIKMTALQ DFFEVKNVSS LLV
//
