ID V9ERV0_PHYPR Unreviewed; 1582 AA.
AC V9ERV0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=glutamate synthase (ferredoxin) {ECO:0000256|ARBA:ARBA00039085};
DE EC=1.4.7.1 {ECO:0000256|ARBA:ARBA00039085};
GN ORFNames=F443_13200 {ECO:0000313|EMBL:ETI41576.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI41576.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI41576.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI41576.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037928}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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:ETI41576.1}.
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DR EMBL; ANIZ01002261; ETI41576.1; -; Genomic_DNA.
DR EnsemblProtists; ETI41576; ETI41576; F443_13200.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT DOMAIN 64..470
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 971..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1582 AA; 173473 MW; A719A3FD4E5BF5F6 CRC64;
MFRIHRRAAT LSSTSGLSSR LSALAPRRSN GVRGFRSIPG EGADKRAIFQ QKGLYRQLEE
KDSCGVGMIA SLKKKPSRST VVQANEMLVR MSHRGGCGCD PASGDGAGML VALPHEFVQR
VVKDGEFGAA AKLLTLEKEK YAVGNVFFNK NAPNDIPLAK KTFDDMAEAM GLKVVGWRAM
PTTSNTLGAT SLASEPHVEQ VMVLNENPNL SGDDFEKELL RLRNVVTSVN EKKFSDFYVN
SLSNRTITYK GQLTPEQLFE YYDDLSAKDF TSYVALVHSR FSTNTFPSWD RAQPNRIMCH
NGEINTLRGN KNWMYARGGT LHSSYFGNRT SDLLPVCSDS KSDSGNFDAV LEILTKASSC
NRSLPEGMMM MIPEAWQNDP LIAPHKKDMY KYQSLLMEPW DGPAMMAFTD GKYIGATLDR
NGLRPSRYYV TKDDHVLLSS EIGVLEHLPE KDIKYKRRLE PGKMFLVDFE RGMIVSDDEV
KKSVSESRPF KKWLDENLVS LSELTVTKKE AAQQKRRPNY AELNRRLNMF GYTTETMDLL
MMPMGIHGKE SLGSMGNDAP LAVLSEQPKL PFEYFKQLFA QVTNPPIDPI REELVMSLMC
PVGPAANVLD ATAEHAKRLM VEHPVMSNAE MGALKSTNNA DWTPKVLDAT FAAGSGARGL
VEALYRLCEQ ATDALVNEKA PIIVLSDKLA GVNRYPVPSL LAVGAVHQHL LRTQQRTSVA
LFAECGDAKE VHDFCTLLGF GADAINPHMA EMALNKMNDE GLLYAHSKKE MANSEVFDKY
RAAVGKGILK VMSKMGISTL QSYKGAQVFE AVGLGDDIIS MCFEGTNSRI QGTDFEALYT
DISRFHEAGY PLHSDMLPLI RNPGSYHFRN DSEIHYNSPK NIVALQRAAR ENSREAYAQY
VEETNELCKR VNLRGLLDFK FVDEDKMPKI EEMESVADIV KRFNTGAMSL GSISQETHEA
LAVAMNTIGG RSNTGEGGED VKRFTKAGGP PNLRRSAIKQ VASGRFGVTM NYLTNADQLQ
IKMAQGAKPG EGGELPGHKV SDYIGSMRHT TPGVGLISPP PHHDIYSIED LAQLIHDLKH
SNPSAEVSVK LVSEVGVGVV AAGVAKAKSD HITVSGHDGG TGAAVWTGVK NGGLPWELGL
AETQQTLVLN DLRSRVKLQT DGQLKTGRDV MVAALLGAEE FGFATGPLIA LGCIMMRKCH
LNTCPVGVAT QDPELRKKFQ GQPEHVVNFM FMLAEEVQDY MRRLGFRKLD DLIGRADLLK
VNQDALHYKS RKLDLSPLLI NASTLNEGAG VKKEMEQDHE VEKCIDMRLI EKAKAALENK
TPVVVEDVAT NLDRTLGATL SHEVCKRYGE EGLPDGTIHL KLKGHGGQSL AFGLAKGVRL
DLEGDSNDYV GKALSGGEVS VFPGEDFSER ANPENVIVGN AVLYGATSGE AYFSGKAGER
FCVRNSGVKA VVEGVGDHGC EYMTGGRVVV LGSTGRNFAA GMSGGIAYIF DEDQTFQEKC
NMGMVGVGPL TETASDAEIQ EVKALITKHL ERTQSPKAQK VLDNWDASVH KFMRVMPSDY
ERVLLQQAAV IKETKKLASA SV
//
