ID A0A1C1CVH7_9EURO Unreviewed; 2152 AA.
AC A0A1C1CVH7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN Name=glt1 {ECO:0000313|EMBL:OCT52513.1};
GN ORFNames=CLCR_09420 {ECO:0000313|EMBL:OCT52513.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT52513.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-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}.
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:OCT52513.1}.
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DR EMBL; LGRB01000008; OCT52513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CVH7; -.
DR STRING; 86049.A0A1C1CVH7; -.
DR VEuPathDB; FungiDB:CLCR_09420; -.
DR VEuPathDB; FungiDB:G647_03910; -.
DR eggNOG; KOG0399; Eukaryota.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000094526; 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; 2.
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; 1.
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:UP000094526}.
FT DOMAIN 53..462
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2118..2152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2119..2152
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 2152 AA; 237725 MW; CE78CB622C595E59 CRC64;
MGSVAEERRQ QEIATEEVQE EYTPYQPEKG YGWGEALPQK QGLYDPGLEK DACGVGFAAN
IKGKASHKII SDARNLLCNM THRGAVGSDA RDGDGAGVMT SIPHKFFVKN FAREVGVELP
PLGQYAAGNL FFKPDTEMLK HATLSFEEAA QSLGLRTLGW REVPRDSTLL GPAALSREPI
ILQPFVVLAS AYGTGNAPEN TDPEQFDDAE FERRLYILRK TVSHDARWKP WFYVCSLSNR
NIVYKGQLAP VQVYQYFHDL VSVDYEGHFA LVHSRFSTNT FPSWDRSQPL RWLAHNGEIN
TLRGNKNWMR AREGVLKSDL FGEEIEKLFP IVEDGGSDSA AFDNVLELLM MNRVLSLPEA
VMMMVPEAWQ GNSAIDPAKA AFYEWAACLM EPWDGPALFT FADGRYCGAN LDRNGLRPCR
YYVTDDDRII CASEVGTIAI EPERVIIKGR LQPGKMLLVD TEAGRIIDDA ELKATVANRQ
PFQQWLNKLL MKMPDVVDAV SKEVDLGYKL SDDSIQEDAR LKAFAYSFEQ VSLLLGPMAA
DSKEALGSMG NDAPLAALAQ QPRLLYEYFR QLFAQVTNPP IDPIREAIVM SLECYVGPQG
NLLEMDESQC GRLLLPSPIL EIETLNAIKN IQTYNPDWSV RTIDITFEKE DGIDGYMKAL
DDICDEATAA IDQGDKVIIL SDRAVSADRV PVSSLLATGL VHHHLIRNKW RSRVALLVET
AEAREVHHMC VLVGYGADGI NPYLAIECIL KMNRQGLIKK KLTDQQIIAN YKASCDGGIL
KVMSKMGIST LQSYKGAQIF EALGIDDTVV DRCFAGTATR VRGMTFELIA QDAFALHEKG
YPSRHVRSIP GLAESGEYHW RDGGEPHIND PVSIANIQDA VRTKNDKSYE AYSLSEYEQI
KHCTLRGMLD FDFDQRAPIP IDQVEPWTEI VRRFVTGAMS YGSISMEAHS TLAVAMNRLG
GKSNTGEGGE DPERSLKMEN GDSMRSAIKQ IASGRFGVTS NYLADSDELQ IKMAQGAKPG
EGGELPGHKV SQSIARTRHS TPGVGLISPP PHHDIYSIED LKQLIYDLKC SNPRARVSVK
LVSEVGVGIV AAGVAKAKSD HILISGHDGG TGASRWTGIK YAGLPWELGL AETHQTLVLN
DLRGRVIVQT DGQIRTGRDV AIACLLGAEE WGFATTPLIA MGCIMMRKCH LNTCPVGIAT
QDPVLREKFQ GTPEHVINFF YYVANELRAI MAQLGLRTVN EMVGRAELLK VREDLRTGKT
QNIDLSLILT PAHSIRPGVA TYNVRKQDHK LHTRLDNKLI SESELALEKG LPCRIETDIV
NTDRALGATL SYQISKRYGE AGLPQDTIHV NIRGSAGQSF GAYLAPGVTL ELEGDSNDYV
GKGLSGGRLI IYPPRSAVFK AEENILIGNV CLYGATSGTC YFRGVAAERF AVRNSGANAV
VEGVGDHGCE YMTGGRVVVL GSTGRNFAAG MSGGIAYVLD MNQDFHSKIN MEMVEVSGVE
TPEEIAFLRG MIEDHHHYTG SELAARILLE FNRALPRFVK VLPTDYKRVL AEQAKQAEEA
KKAEYPLPIL PGNPVRNLHQ EQREIRHDKE AKQQKANMLD IEEGVNGDAG QAKHKAALVL
DKTRGFMKYA RRAEKYRNPK TRVKDWAELN SRLNEDELKY QSARCMDCGV PFCQSDTGCP
ISNIIPKWNE LVFQDQWKDA LNRLLMTNNF PEFTGRVCPA PCEGACVLGI TDDPVGIKSI
ECAIIDKGFE MGWMVPDPPQ ERTGKTVAII GSGPAGLAAA DQLNRVGHTV TVYEKSDRAG
GLLMYGIPNM KLDKRIVQRR IDFMAAEGVQ FKTGVMVGPG EEVSLDSLRQ EYDAVVISTG
AQVPRDLKIK NREAEGIHFA MEFLHANTKS LLDSELGDGH YISAKDKHVI VIGGGDTGND
CIGTSLRHGA KSITNFELLP QPPPERARDN PWPQWPRIYR VDYGHTEVKQ HYGKDPREYC
VMTKDFDVKD GRIVGINTNR VDWTKSATGG WDMKPREGSE EYFPADLVLL SMGFLGPDDR
LFEGQVELDP RKNIKTPKNM YNTNLPGVFA AGDCRRGQSL IVWGINEGRQ CARQVDSFLM
GEGSILPVTG GIIQRAQHDA VPRPKESKAH KGGDMAHAAE DFKRGTEIKV GA
//
