ID M2Y621_GALSU Unreviewed; 991 AA.
AC M2Y621;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Asparagine synthase (Glutamine-hydrolysing) {ECO:0000313|EMBL:EME31438.1};
DE EC=6.3.5.4 {ECO:0000313|EMBL:EME31438.1};
GN ORFNames=Gasu_13990 {ECO:0000313|EMBL:EME31438.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME31438.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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DR EMBL; KB454492; EME31438.1; -; Genomic_DNA.
DR RefSeq; XP_005707958.1; XM_005707901.1.
DR AlphaFoldDB; M2Y621; -.
DR STRING; 130081.M2Y621; -.
DR EnsemblPlants; EME31438; EME31438; Gasu_13990.
DR GeneID; 17090083; -.
DR Gramene; EME31438; EME31438; Gasu_13990.
DR KEGG; gsl:Gasu_13990; -.
DR eggNOG; KOG0573; Eukaryota.
DR OrthoDB; 168254at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR005052; Lectin_leg.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR45937; ASPARAGINE SYNTHETASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR45937:SF1; ASPARAGINE SYNTHETASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00733; Asn_synthase; 1.
DR Pfam; PF03388; Lectin_leg-like; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Ligase {ECO:0000313|EMBL:EME31438.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 957..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..215
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 816..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 991 AA; 112117 MW; 447FF7DCE4E9C89C CRC64;
MCGIFAILSG VQGLFDSFQP FTCNCTHFTQ VKQQWKDATR DFLQRRGPDS FRIKCYSLYF
QRSLELQAAV LSLRGNRVVE QPLEDSFGNV LLFNGEIYDD NMNQEENDTL VLSKLLGQLV
FRHRNSGRDN NWKPLYSDIL ELLDSLPGPW SIIYYISSLR CLIFGRDVIG RRSLLLGKTG
DDQSIFISSV SPQEAACSGC LIELAPLGLY CIEWEEDNPF GRLDCHFRDV RKRNISTSSL
LSCRLPRGAP QHALFLDSYL PDKWWRTQEI SVHSLDDTSN FVLAWINVLL RAVGRRIEML
QLPSQSSSNR CGSLPFALLF SGGIDSLVLA YLIWKVCQSH EIYQYKTLEL INVCFGPPSK
SPDRKTAMEG IEELNRICSN HKLKMPFRLL FVDVDKEEYQ KYRQHLKYLL FPCCTPMDIS
IGSTLWFGAR AQGHVKESND VHSNPYTSSS KVLLSGLGAD ELLGGYKGRH RSVFQRGGYS
TLAYELNMDL SRLWWRNLGR DDRIVGDHGK ELRLPFLDEQ VIDFITSLPL QVICDMELPD
GIGDKRILRQ AAKQLGFSND FVSRKKRAMQ FGSMIAAQLQ LPYLLPADPL YSFRSPLSPP
VIPGEVLRNW FGVGQTKLAQ KDGVDIVRLT DMEQDAFGTL YHITPLKQQH FNLSFVYWIG
TKEIQPRVDS LAFWYTKHPP TYGTVYGNEA AFQGLGIVIQ LFDNQWHRPS LFPVVNERTT
KGSDWQVKVL SPGCALGSLT GKIYVSYQQG KLSVYQLPIQ KNTLPNPEFC FDVQLPPSAQ
LDSGYFGFTA KSGNYATEHS IIQVTVATGA VTTAAKNTAD RNKKQPDPFD KASKKSVVDG
QKTSSVLSPP KPVASSSKPK PATQSNSMLN AVPSQRDPQT PANVQGVKTD STAQQEGNQQ
MQMNHEGPQD SMNSNPNMEY LKSIWDDTHE KQQDLSAKLT QLLVEWETMK RSTSITMIFA
IALVVLLQFY ACMLYLYYRK LASRLRYNKI I
//
