ID A0A1Y2G9T1_9FUNG Unreviewed; 2094 AA.
AC A0A1Y2G9T1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=BCR41DRAFT_425774 {ECO:0000313|EMBL:ORZ04870.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ04870.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ04870.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ04870.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORZ04870.1}.
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DR EMBL; MCFF01000054; ORZ04870.1; -; Genomic_DNA.
DR STRING; 64571.A0A1Y2G9T1; -.
DR InParanoid; A0A1Y2G9T1; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000193648; 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:UP000193648}.
FT DOMAIN 36..434
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 929..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 36
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT BINDING 1154
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1160
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1165
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2094 AA; 230266 MW; 0411EB69D014203B CRC64;
MEAFMNKNNV ESNNSWAGAL PIAQGLYNPE NEKDSCGVGF IANIKGELSH RILKDASSIL
CNMTHRGATS ADPRDGDGAG VMTGMPHTFM VEEATRLNIT LPAQGEYAVG NVFLRPDEPH
VHEQKSTFES IAQQNGLKVL GWRLVPVDNS ILGPAAKSRE PSIQQPFVIL DPAVYNKFDN
KRFQRQLYLL RKQATHAITL KNWFYICSLS NQNIVYKGQL SPVQVYDFFY DLQNHKFLTH
FALVHSRFST NTFPSWDRAQ PMRWAAHNGE INTLRGNKNW MRAREGVMHS DYFGSDLQKL
FPIIEEGGSD SSAFDNVLEL LVVNGVLSLP EAIMMMLPEA WQSNTNMEPE KKAWYEWAAC
LMEAYDGPAL MTFSDGRYCG ASLDRNGLRP CRFYKTTDGL MICASEVGTL NIAPERILEK
GRLQPGKMLL VDTLEGRVVD DRELKLSIAA RQNFRQWVDE QMLSMTDAVA NAPKFDLMSS
IDDVPLTQDP RLPAFKLTIE QLNLLLMPMT TDGKEALGSM GNDAPLACLA TEPQIIFDYF
RQLFAQVTNP PIDPIREEIV MSLECYVGPE GNILEMDQSQ CHKLKLPTPI LSLNEMEAIK
NFDITRADWK TRVIDITFPK SDGPAGYVPC LERICEQVSA AIEDGVKIVV LSDRGVSAER
VALSSLIATG GVHHYLVREK KRSRVAIGVE TAEAREVHHA CVLLGYGADM ICPYLAQEAI
LKLYRENSLR SDAGPEKLLK NYIKATSNGI LKVMSKMGIS TLQSYKGAQI FEALGLDEPV
IARSFAGTAS RIKGVGFDLL ALDAFALHER AWPSRDTITV EGIPESGEYH WRNGAIPHIN
DPHGIANLQD AVRRKNDSAY EAYSQNAFEQ IKNCTLRGML EFDFNKRKPI PIDEVEPWTE
ICKRFCTGAM SYGSISMEAH STLSIAMNRI GGKSNSGEGG EDPARSNPRE NGDSLRSAIK
QIASGRFGVT SYYLADADEI QIKMAQGAKP GEGGELPGHK VSDEIGKTRH STPGVGLISP
PPHHDIYSIE DLKQLIYDAK AANPRARISV KLVSEVGVGV IASGVAKAKA DHILISGHDG
GTGASRWTGI KYAGLPWELG LAESHQTLVL NDLRGRVVVQ TDGQIRTGRD VAIACLLGAE
EWGFATTPLI ALGCTMMRKC HLNTCPVGVA TQDPYLREKF AGSPEHVINF FYYVAEELRT
IMAKLGFRTI NEMVGRTDVL CVDESRRNAK NANIDLTPIL TPAFTLRPGA ATYKVRKQEH
MHHTRLDNKF ISEAQDALNT GKRVELDGKV VNTDRALGTT ISYHVSNKYG ESGLPDDTIH
ISLKGSAGQS LGAWLAPGVT IELEGDSNDY VGKGLSGGRL IIYPPKNSSF KSEDNVIIGN
TCLYGATSGK AFFSGIAAER FAVRNSGATA VVEGTGDHGC EYMTGGRVIV LGSTGRNFAA
GMSGGIAYVL DLKGDFKSKV NMEMVAFETV NDTEEIAWFK DTLEDHRHYT GSAIADRILK
NLGEYLPKIV KVMPTDYKKV LEAQRAAKLA AAAPKPDIIT PVLTASPLAA KPKPNEPALV
DLEDSMVDAE TYKKRSEMVD KVRGFMKYKR RGDAYRNPKK RTKDYKEISA RLSDGELQVQ
AARCMDCGVP FCQSNTTGCP IGNIIPKWND LVFKDQWEEA LNRLLMTNNF PEFTGRVCPA
PCEGSCVLGI NELPVAIKSI ECAIIDRGFE MGWMKPRPPT HRTGRKVAII GSGPAGLAAA
DQLNKAGHTV TVYDRNDRFG GLLMYGIPNM KLDKGIVQRR IDLMAAEGIS FVPNAHVGVT
HDVNEIRKQS DALILATGAT WPRDLPIANR NLDGIHFAME FLQLNTQSLL DSELNDGKYI
SAKGKHVVVI GGGDTGCDCI ATSLRHGAAS IVNFELLPQP PATRAKDNPW PQFPRVFKQD
YGHSEVQSHF GKDPREYSIV TKEFVSDGNG KVKGLNTIRV EWTQDASGRW SMKEMAGTEQ
YFQADLVLLS MGFLGPEAEL LKAVGCKLDG RTNIETPKDS YRTSVSNVFA AGDARRGQSL
IVWGINEGRQ CAREVDEFLV GNTLLPVTGG IQQRSLKSLT MEAYQNTTTP VAAS
//
