ID A0A093Z2V2_9PEZI Unreviewed; 2993 AA.
AC A0A093Z2V2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=V492_04330 {ECO:0000313|EMBL:KFY11661.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY11661.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY11661.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY11661.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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|ARBA:ARBA00001927};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFY11661.1}.
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DR EMBL; JPJU01001425; KFY11661.1; -; Genomic_DNA.
DR STRING; 1420902.A0A093Z2V2; -.
DR HOGENOM; CLU_000422_8_0_1; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; 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 CDD; cd07892; PolyPPase_VTC2-3_like; 1.
DR CDD; cd14480; SPX_VTC2_like; 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 Gene3D; 3.20.100.30; VTC, catalytic tunnel domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR003807; DUF202.
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; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR018966; VTC_domain.
DR InterPro; IPR042267; VTC_sf.
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; PF02656; DUF202; 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 Pfam; PF09359; VTC; 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.
DR PROSITE; PS51382; SPX; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Coiled coil {ECO:0000256|SAM:Coils}; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 2899..2917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2937..2957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..463
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 2208..2355
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REGION 963..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2394..2416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2784..2813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2269..2326
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2787..2803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2993 AA; 332331 MW; 01F0299E64835E45 CRC64;
MGRADDFDDR HIQTAAENEP YNQYEYQTKD NESWAGALPV KQGLYDPALE KDACGVGFTC
HIKGKPSHKI VSDARNLLCN MTHRGAVGSD ARDGDGAGVM TSIPHKFFIK NFERETDIKL
PPLGQYAVGN LFFKPDEEVL QDSKNQLVNI AESLGLRILG WREPPRDSTI LGPAAASREP
VILQPFVVLT SAYGLGNSPE TTDPDQFDEK LFERQLYVLR KRATHTIGPH NWFYLCSLSN
KNIVYKGQLA PIQVYQYYYD LVNADYEGHF ALVHSRFSTN TFPSWDRAQP LRWAAHNGEI
NTLRGNKNWM RAREGVMQSD VFGDELEELY PIVEHGGSDS AAFDNVLELL TINGVLSLPE
AVMMMVPEAW QDNPAMDPAK AAFYEWAACQ MEPWDGPALF TFADGRYCGA NLDRNGLRPC
RYYILDDDRI ICASEVGTIS VDPERVVQKG RLQPGKMLLV DTLAGRIIDD AELKATVSNR
QDFRAWLQDQ LISLPKIHDN LVAGGTLDLA PKPTSHAIQE DPMLKAFGYT FEQVSLLLGP
MATDEKEALG SMGNDAPLAC LAQAPRLLYE YFRQLFAQVT NPPIDPIREA IVMSLECYVG
PQGNLLEMDA SQCSRLLLPT PVLSINELNA LKDITKLHSQ WTVKIIDLTF KKEEGVQGYI
KHLDYICSEA TAAIENKDRI IILSDRATSV DRVPVSALLA CGMVHHHLVN NKWRSLAAIV
VETAEAREVH HMCVLLGYGA DAINPYLAME CILKLNREGL IRKKLSDDTL IRNYKYSADG
GILKVMSKMG ISTLASYKGA QIFEALGVDD SVVERCFKGT ATRIRGITFE QIAEDAFRFH
EQGFPSRSTT SIPGLPESGE YHWRDGGEPH INDPTSIANI QDAVRTKNDK SYEAYSLSEY
EQIKSCTLRG LLDFKFDECT PVPIDQVEPW TEIVRRFCTG AMSYGSISME SHSTLAVAMN
RLGGKSNTGE GGEDPERSKQ MANGDTMRSA IKQVASGRFG VTSNYLADSD EIQIKMAQGA
KPGEGGELPG HKVSKSIART RHSTPGVGLI SPPPHHDIYS IEDLKQLIYD LKCSNPRARV
SVKLVSETGV GIVASGVAKA KADHILISGH DGGTGASRWT GIKYAGLPWE LGLAETHQTL
VLNDLRGRVV VQTDGQLRTG RDVAIACLLG AEEWGFATTP LIAMGCIFMR KCHLNSCPVG
IATQDPELRK KFKGTPEHVI NFFYYIANEL RAIMAKLGFR TINEMVGHAE VLRVRDDLRT
PKTANIDLSL ILTPAHQLRP GVATFNVRKQ DHRLYVRLDN KLISEAELTL DKGLPSRIEC
DVINTDRAMG TSLSYQVSKR YGEEGLPMDT VHVNIKGSAG QSFGAFLAPG VTLELEGDAN
DYVGKGLSGG RLIIYPSRAA VFKAEENVIV GNVCLYGATG GSVFFRGMAA ERFAVRNSGV
TAVVEGVGDH GCEYMTGGRV LILGSTGRNF AAGMSGGIAY VLDIHQDFMS KLNMEMVEAS
AIDDPAEIAF VRGLVEDHHH YTGSELAARI LLDFNRALKR FIKVLPVDYK RVLAEEAAKA
AEAKKAEYQL PLLQGAQGKG SREGTSGGNH VHGKKQDLQD IEETVGDAAA EKKRSLVLDK
TKGFMKYQRR SEKYRSAKTR TRDWAELSKR LDEDELKYQA ARCMDCGVPF CQSDSGCPIS
NIIPKWNELV FQNQWKDALN RLIMTNNFPE FTGRVCPAPC EGACVLGINE DPVGIKSIEC
AIIDRGFDMG WMVPQPPKVR TGKRVAIIGS GPAGLACADQ LNKAGHLVTV YERADRLGGL
LMYGIPNMKL DKAIVKRRTD FMAAEGIIFK TGVAVGEDVE LLGLRKDNDA VVIATGATVA
RDLPIKNRNL EGIHFAMQFL HKNTKSLLDS NLDDGSYISA KGKNVVVIGG GDTGNDCIGT
SLRHGAKSVT NFELLPQPPP ERARDNPWPQ WPRIYRVDYG HTEVKQHMGK DPREFCVMSE
DFVDDGNGVV KGINTIRVEW TKSATGGWDM KKIDGSQQFF PAELVLLSMG FLGPEDRVLG
DEIEKDARKN VKTPPGKYST NVDGIFAAGD CRRGQSLIVW GINEGRSCAR ECDMFLENSS
LLPVTAVVAV YSVFVDKYME HDQNDGMDVG PKTAYRRIWH NSNIAATSNR YMSDDSSAVA
LIAIAVTWLQ QIDTSPIDDN RTCAAHYTSR KEAEAQGRLC FQRYDVRMRF GQTLANSVHE
PWKEQYLDYA KLKKLLREDG AGDDNKPWTE DDESRFCEEI LNTQLGKVAA FQESTFQKLE
ERANNVSDRL KDLAPQGADK VDVAKFKEIE DELDSITNEA NQLKKYSALN YTGFLKIVKK
HDRKRGNKYK VRPMLQINLS KRPFNSEQAY TPIINKLSIM YFIVRQHLED KADKGLPSVG
DRKTSSTIDM PPQPHPQNRE KYTAYKFWVH PDNLLEVKTY ILRRLPVLVY SEQSANQADA
SQGDPTITSL YFDNSQFGLY SQKVDGTVDA SSLRVRWYGK LNDKPELLLE QKTIHGAGNS
EEKRFPIKEK YVQPFITGEY DMGKNVQKLE RQGQPEEKVA DYQRSVNEIQ EFIKDRNLQP
VLRANYTRTA FQKPLDDRVR ISIDTELAFI REDSLDSDRP CRNPNSWHRT DIDNTQMEFP
FPNVNQGEIS RFPYAVLEIK VKENSGKKTP QWVQDLMASH LVHKAPRFSK FVHGIASLFE
DYVNSLPFWL SDVETDIRKD PHAAFAEEEL AKAQKAEDEL LVGSYMASAS NVKGSYKAAL
GSPLSKSYMT DRFASESAAK SRAMADAASK GKGKGRAQEN EDGDQDAGGI SGYGTTSSVF
PSFSLSRYAQ SRRQHKAALP PGVTKPGILI KDSGPLQVEP KVWLANERTF LKWQHICILL
GSLAVSLYTA AGENTLAEYM GIAYIIIAAF AGLWGYYIHF VRRNMIIARS GKDFDNFVGP
LVVSFALLVA LLLNFGFKYN AALERIGQDR QGINGTATGA QSAGNDIHSE LVR
//
