ID A0A0D1YS55_9EURO Unreviewed; 2150 AA.
AC A0A0D1YS55;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=PV08_02338 {ECO:0000313|EMBL:KIW18051.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW18051.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW18051.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW18051.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024267};
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|PIRSR:PIRSR000187-2};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|PIRSR:PIRSR000187-2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004944}.
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}.
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DR EMBL; KN847493; KIW18051.1; -; Genomic_DNA.
DR RefSeq; XP_016238267.1; XM_016376697.1.
DR STRING; 91928.A0A0D1YS55; -.
DR GeneID; 27329421; -.
DR VEuPathDB; FungiDB:PV08_02338; -.
DR HOGENOM; CLU_000422_8_0_1; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR012220; Glu_synth_euk.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
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; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000187; GOGAT; 1.
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; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|PIRSR:PIRSR000187-2};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
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, ECO:0000256|PIRSR:PIRSR000187-
KW 2}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT DOMAIN 53..462
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2119..2150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 53
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT BINDING 1183
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1189
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1194
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2150 AA; 237899 MW; DA25BA1F4F43279D CRC64;
MGLPTVDSHK QENETPEVQE EYTPYQPEKG YGWGEALPEK QGLYDPSLEK DACGVGFAAH
IKGKPSHKIV SDARNLLCNM THRGAVGSDA RDGDGAGVMS SIPHKFFVKN FAREVGVELP
PLGQYAAGNL FFKPDTEMLK HATLSFEEAA QSLGLRTLGW REVPRDSTLL GPAALSREPI
ILQPFVVLAS AYGTGNKPDI TDPEQFDDVE FERKLYILRK TVSHDPRWKP WFYVCSLSNR
NIVYKGQLAP VQVYQYYHDL VSVDYEAHFA LVHSRFSTNT FPSWDRSQPL RWLAHNGEIN
TLRGNKNWMR AREGVLKSDL FGEDLEKLFP IVEDGGSDSA AFDNVLELLV MNRVLSLPEA
VMMMVPEAWQ GNTAMDAGKA AFYEYAANLM EPWDGPALFT FSDGRYCGAN LDRNGLRPCR
YYVTDDDRII CASEVGTIAI EPERVIIKGR LQPGKMLLVD TQAGRIIDDA ELKATVANRQ
PFQQWLDKNL MKMPQVYEAL SKEADLSSKL TESSVQEDAR LKAFGYSFEQ VSLLLAPMAA
DSKEALGSMG NDAPLACLAQ QPRLLYEYFR QLFAQVTNPP IDPIREAIVM SLECYVGPQG
NLLEMDESQC GRLLLPSPIL ETETFNALKN INLYNKDWSV RTIDITFEKS AGVDGFMNAL
DSICDSATAA IEEGDKIIIL SDRATSADRV SVPTLLATGL VHHHLVRNKW RSRAAIIVET
AEAREVHHMC VLLGYGADGI NPYLAIECIL KLNREGIIKK KLTDQQLIAN YKASCDGGIL
KVMSKMGIST LQSYKGAQIF EALGIDDAVV DRCFAGTATR VRGMTFELIA EDSFAFHEQG
FPSRHVRDIP GLPETGEYHW RDGGENHIND PVSIANIQDA VRTHNDKSYE AYSLSEYEQI
KNCTLRGMLD FDFDQRQPVP IDQVEPWTEI VRRFVTGAMS YGSISMEAHS TLAVAMNRLG
GKSNTGEGGE DPERSLKMEN GDSMRSAIKQ IASGRFGVTS NYLADADELQ IKMAQGAKPG
EGGELPGHKV SEPIARTRHS TPGVGLISPP PHHDIYSIED LKQLIYDLKC SNPRSRVSVK
LVSEVGVGIV AAGVAKAKAD HILISGHDGG TGASRWTGIK YAGLPWELGL AETHQTLVLN
DLRGRVIVQT DGQIRTGRDV AIACLLGAEE WGFATTPLIA MGCIMMRKCH LNTCPVGIAT
QDPLLRKKFQ GTPEHVINFF YYIANELRAI MAQLGFRTVN EMVGRAELLK VREDLRSRKT
ENLDLSLILT PAHSIRPGVA TYNVRKQDHK LHTRLDNKLI SESELALEKG LPCRIETDIV
NTDRTLGATL SYHISKRYGE AGLPQDTIHV NIRGSAGQSF GAYLAPGVTL ELEGDANDYV
GKGLSGGRLI VYPPRSAVYK AEENILIGNV CLYGATSGTC YFRGVAAERF AVRNSGANTV
VEGVGDHGCE YMTGGRVVVL GSTGRNFAAG MSGGIAYVLD MNQDFHSKIN MEMVEVSGVD
DPSEIAFLRG MIEDHHHYTG SELAARILLE FNRALPRFVK VLPTDYKRVL LEQAKKAEEA
KKAEYPLPIL PGNPVRNLHQ EQRDAAHEKE AKQKKAEMLD IEEGINGDAD KAKQKAALVL
DKTRGFMKYT RRSEKYRNAK TRVKDWAELS SRLNEDELKY QSARCMDCGV PFCQSETGCP
ISNIIPKWNE LVFQNQWKDA LNRLLMTNNF PEFTGRVCPA PCEGACVLGI NEDPVGIKSI
ECAIIDKGFE MGWMVPTPPA ERTGKKVAII GSGPAGLAAA DQLNRVGHSV TVYEKSDRCG
GLLMYGIPNM KLDKRIVQRR VDFMAAEGVN FVTGVMVGPG EEITLESLRK SNDAVIISTG
AQVPRDLKIK NREAEGVHFA MEFLHANTKS LLDSELGDGK YISAKDKHVI VIGGGDTGND
CIGTSLRHGA KSITNFELLP QPPPERARDN PWPQWPRIYR VDYGHTEVKQ HYGKDPREYC
VMTKDFVMED GRVVGINTNR VEWTKSATGA WEMKPKEGSE QYFPADLVLL SMGFLGPDDR
LFESEIELDP RKNIKTPKNM YNTNIPGVFA AGDCRRGQSL IVWGINEGRQ CARQVDSFLM
HTGSVLPVTG GIVRRAQHDS VPPPRESKAH KQGDMAHASE EMKRVPEIKA
//
