ID   A0A9C7Q3J3_9RHOD        Unreviewed;       559 AA.
AC   A0A9C7Q3J3;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   13-SEP-2023, entry version 3.
DE   RecName: Full=Glutamine amidotransferase type-2 domain-containing protein {ECO:0000259|PROSITE:PS51278};
GN   ORFNames=GpartN1_g7619.t1 {ECO:0000313|EMBL:GJQ15828.1};
OS   Galdieria partita.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=83374 {ECO:0000313|EMBL:GJQ15828.1};
RN   [1] {ECO:0000313|EMBL:GJQ15828.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 102759 {ECO:0000313|EMBL:GJQ15828.1};
RX   PubMed=36194630; DOI=10.1073/pnas.2210665119;
RA   Hirooka S., Itabashi T., Ichinose T.M., Onuma R., Fujiwara T.,
RA   Yamashita S., Jong L.W., Tomita R., Iwane A.H., Miyagishima S.Y.;
RT   "Life cycle and functional genomics of the unicellular red alga Galdieria
RT   for elucidating algal and plant evolution and industrial use.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
RN   [2] {ECO:0000313|EMBL:GJQ15828.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 102759 {ECO:0000313|EMBL:GJQ15828.1};
RA   Hirooka S., Miyagishima S.Y.;
RL   Submitted (JAN-2022) 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:GJQ15828.1}.
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DR   EMBL; BQMJ01000075; GJQ15828.1; -; Genomic_DNA.
DR   Proteomes; UP001061958; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01991; Asn_Synthase_B_C; 1.
DR   CDD; cd00712; AsnB; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR006426; Asn_synth_AEB.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR033738; AsnB_N.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR01536; asn_synth_AEB; 1.
DR   PANTHER; PTHR11772; ASPARAGINE SYNTHETASE; 1.
DR   PANTHER; PTHR11772:SF2; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING]; 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   PIRSF; PIRSF001589; Asn_synthetase_glu-h; 2.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW   Asparagine biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001589};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PIRSR:PIRSR001589-1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001589}.
FT   DOMAIN          2..197
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001589-1"
FT   BINDING         101
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT   BINDING         351..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT   SITE            353
FT                   /note="Important for beta-aspartyl-AMP intermediate
FT                   formation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001589-3"
SQ   SEQUENCE   559 AA;  63598 MW;  CFCAA28A8020416D CRC64;
     MCGILAVLGS TLPVEQLREL VKSCTKKLYH RGPDEEQYFV SEDGWCGLGF ARLKIVDPEH
     GAQPMFNDER TVWSVTNGEL YNHEEIREKE LDRMTLHSHS DCEVVIPLYE KYVATQLYDH
     DIQYLYNLLR GVFASCVVDL KRGFFMAGRD PIGVRALFYG TSKDGAVWFA SEAKAIVDVC
     DYVTAFIPGT FIKGYRGREQ ENSFTRYYEP VFWNDNWMPV SPVDYQLLHD TFVLSCKRRL
     MSDVPVGVFI SGGLDSSLVA SVAKRLLGPH YEFHSFACGL EGAPDVAAAQ KVADFLGTKH
     HVLTFTVEEG IKALDDVIYH LETYDVTTVR ASTPMYLLSG LCKKYVKVVL SGEGADEIFG
     GYLYFHNAPN ETAFHQETVR RVKLLYTADV LRGDRATAAQ SLELRVPFLD RDFLDVAMSI
     HPHEKVTCKN RIEKYIIRYA FSKEFCGEVY LPDDILWRQK EQFSDGVGYS WIDGLKAYCE
     KAVTDQDMQN ASQRFPHDTP TTKEAYVYRV LFEKHFGKSR AVQGLRESIA RWVPMWSDST
     DPSGRAQRVH VAAYSNGEQ
//