ID C8VEZ6_EMENI Unreviewed; 2126 AA.
AC C8VEZ6;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=ANIA_05134 {ECO:0000313|EMBL:CBF80924.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF80924.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; BN001305; CBF80924.1; -; Genomic_DNA.
DR STRING; 227321.C8VEZ6; -.
DR EnsemblFungi; CBF80924; CBF80924; ANIA_05134.
DR VEuPathDB; FungiDB:AN5134; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; C8VEZ6; -.
DR OMA; WDGPAAM; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000000560; Chromosome V.
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; IMP:AspGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0009064; P:glutamine family amino acid metabolic process; IMP:AspGD.
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:UP000000560}.
FT DOMAIN 53..462
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 961..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..982
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 1184
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1190
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1195
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2126 AA; 234235 MW; 17F1FDEEBCC62A57 CRC64;
MGLNLEEIYG QTIVEEQRPN EYSEYQPKKG YGWANTLPER QGLYDPEYEK DACGVGFAAN
IKGKASHKIV SDARNLLCNM THRGAVGSDA RDGDGAGVMT SIPHKFFIKN FAREVGVDLP
PLGQYAVGNL FFKPDEEALK ESIKQFEEIA TSLGLRVLGW REVPRDSTIL GPAALSREPT
ILQPFVVLKS AYGEGNKPDI TDPEQFDTKT FELQLYVLRK RATHIIGLAN WFYLCSLSNR
NIVYKGQLAP IQVYQYYHDL VNVDYEGHFA LVHSRFSTNT FPSWDRAQPL RWAAHNGEIN
TLRGNKNWMR AREGLLKSDI FGEELESLLP IVEDGGSDSA AFDNVLELLM INGVLSLPEA
VMIMIPEAWQ DNPAMDPAKA AFYEWAACQM EPWDGPALFT FSDGRYCGAN LDRNGLRPCR
FYVTDDDRII CASEVGAVDI DQERVVQKGR LQPGKMLLVD TVAGRIIDDS ELKYTVAHRH
DFSSWLNKEL VKLPAITEKL VEQNMDLRHD LDNTTVQNDP RLKAFGYSFE QVTLLLGPMG
ADSKEALGSM GNDAPLACIA KQPRLLYEYF RQLFAQVTNP PIDPIREAVV MSLECYVGPQ
GNLLEMDPSQ CRRLLLPSPI LSIPEFNALK NINTVHKDWT VRLIDITFEK KKGVPGYIEA
LDRICDAATE AIQQGDKILI LSDRATSADR VPVSALLATG LVHHHLVRNK WRSLAALIVE
TAEAREVHHM CVLVGYGADG INPYLAMECI LKMNREKLIR KELSDEKVIE NYKASCDGGI
LKVMSKMGIS TLASYKGAQI FEALGIDDSV IDRCFTGTAS RIRGMNFELI AQDAFAIHER
GYPSRAIVDI PGLNESGEYH WRDGGEDHIN DPVSIANIQD AVRTKNDKSY EAYAKAAHEQ
IKNCTLRGML EFDFDQRTPI PIDQVEPWTE IVRRFVTGAM SYGSISMESH STLAVAMNRL
GGKSNTGEGG EDPERSKRME NGDTMRSAIK QIASGRFGVT SHYLADADEL QIKMAQGAKP
GEGGELPGHK VVGPIAHTRY STPGVGLISP PPHHDIYSIE DLKQLIYDLK CSNPRARVSV
KLVSEVGVGI VASGVAKAKA DHILISGHDG GTGASRWTGI KYAGLPWELG LAETHQTLVL
NDLRGRVIVQ TDGQIRTGRD VAVACLLGAE EFGFATTPLI AMGCIMMRKC HLNTCPVGIA
TQDPELRKKF EGQPEHVINF FYYIANELRA IMAKLGIRTI NEMVGRAELL KVRDDLTNPK
QENIDLSLIL TPAHSLRPGV ATYNVRKQDH RLHTRLDNKL IAESELALEK GLPCRVECDV
VNTDRALGAT LSYQVSRRYG GEGLPQDTIH SNIKGSAGQS FGAYLAPGIT LELEGDANDY
VGKGLSGGRL IVYPPRGAAF KAEENVIVGN TCLYGATRGT CFFRGVAAER FAVRNSGATA
VVEGVGDHGC EYMTGGRVVV LGSTGRNFAA GMSGGIAYIL DMNQDFLSKV NMEMVECSGL
EDPAEIAFLR GLIEDHHHYT GSELAARILL DFTRALPHFI KVLPTDYKRT LEEEAAKAAA
AKKAETTIPQ LPSVPVEKQK PKAEGDAKKA ELLDIEDSVT DSKVEKKRTA LILDKTRGFM
KYNRRSEKYR NPATRTRDWA ELSSRLTEDE LKYQSARCMD CGVPFCQSDT GCPISNIIPK
WNELVFQNQW QDALNRLLMT NNFPEFTGRV CPAPCEGACV LGINEDPVGI KSIECAIIDR
GFEMGWMVPR PPPVRTGKTV AIIGSGPAGL AAADQLNRVG HSVTVYERAD RIGGLLMYGI
PNMKLDKKIV QRRVDLMAAE GVKFVTGVSV GPDSEVSLDS LRKSNDAVII ATGATVARDL
KVPGRELEGI HFAMQFLHKN TKSLLDSELA DGAYISAKDK HVVVIGGGDT GNDCIGTSVR
HGAKSVVNFE LLPQPPPERA RDNPWPQWPR IYRVDYGHSE VKTHMGKDPR EYCIMSKEFV
DDGNGRVKGI NTVRVEWTKS ATGGWDMKTV EGSEQFFPAD LVLLSMGFLG PEDRLLGEEI
ERDARKNVKT PPGHYGTNVP GVYAAGDCRR GQSLIVWGIN EGRQCAREVD TFLSGISSQL
PVTGGIVRRP AVDAVRQATE TVTIAA
//
