ID A0A1B7T8G5_9ASCO Unreviewed; 909 AA.
AC A0A1B7T8G5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glutamate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HANVADRAFT_4179 {ECO:0000313|EMBL:OBA25014.1};
OS Hanseniaspora valbyensis NRRL Y-1626.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA25014.1, ECO:0000313|Proteomes:UP000092321};
RN [1] {ECO:0000313|Proteomes:UP000092321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:OBA25014.1}.
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DR EMBL; LXPE01000289; OBA25014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7T8G5; -.
DR OrthoDB; 20503at2759; -.
DR Proteomes; UP000092321; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 2.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092321}.
FT DOMAIN 87..275
FT /note="Glutamate synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01493"
FT DOMAIN 428..537
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 551..725
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 799..871
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT COILED 381..408
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 909 AA; 99677 MW; 09A4D6E6251464ED CRC64;
MAKLGYRTVD EMVGRSEKLK RYAKTTTKNI NIDLDPILTP AHIIRPGVAT RYVKKLENKM
FARLDNKLVD EAEITLDKGL PVSIDASIIN TDRALGATLS YRVSKRFGPE GLPQDTIVVN
LKGSAGQSFG AFLAPGISFI LDGDANDYVG KGLSGGQIVI RPPENSKFKS DENVIAGNTC
FYGATSGRAF LSGCAGERFA VRNSGATIVV EKIIGNNAFE YMTGGRAVVL SQLDSINAFS
GCTGGIIYCL TSDHDSFKSK INSDSVELHS LDDPVEIAFV KNLIQEHYHL TKSELANRIL
NNFNHYLSSF IKVFPTDYKT VLEQQAKEAA AAALRSKNSY LKKLEKNGVV VDATNGEVDI
VATKRQKLAK SVVASHQATL HEAKVADLED AVQDADQLEK KAEKLDKIKG FKKYKLRHEA
YRDASSRTDD WNEISDSITK KDAKYQTARC MDCGVPFCTS DTGCPVSNVI PKFNELVFKN
QWKLALEKLL ETNNFPEFTG RVCPAPCQGA CTLGINNDPV GIKSVERVII DNAFKEGWIK
PQPPMHRTGK TVAIIGSGPS GLASADQLNR AGHTVTVYER NDRCGGLLMY GIPNMKLDKS
VVQRRVDLLA AEGINFVTGC AVGKDITIEE LKNKHDAVIY AIGSTIPRDL RLPGRDLKNI
DFAMTLLEAN TKALLAKDLE TMRENIKGKK VVVIGGGDTG NDCLGTAVRH GAASVVNFEL
LPQPAKERTN DNPWPQWPRI MRVDYGHAEV KEHYGRDPRE YCILSKEFIG NENGEVTAIK
TVRVEWNKSQ SGVWQMVEIP GSEEIFEADI ILLSMGFVGP ELIEDASIKK TNRGTIGTVS
DASYCVDDSN VFACGDCRRG QSLIVWAIQE GRKCAREVDT FLIGNTVLPG NGGIIKRDYK
MLEELAAQA
//
