ID A0A0L6VIW6_9BASI Unreviewed; 2132 AA.
AC A0A0L6VIW6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-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 ORFNames=VP01_150g3 {ECO:0000313|EMBL:KNZ60726.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ60726.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ60726.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ60726.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-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:KNZ60726.1}.
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DR EMBL; LAVV01005665; KNZ60726.1; -; Genomic_DNA.
DR STRING; 27349.A0A0L6VIW6; -.
DR VEuPathDB; FungiDB:VP01_150g3; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000037035; 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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; 1.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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:UP000037035}.
FT DOMAIN 49..449
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT BINDING 1172
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1178
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1183
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2132 AA; 234007 MW; CD4677AB4739D09C CRC64;
MATKVHTNQQ PKEQNSESDT HVIRSSNHWA GALPAPQGLY DPEQEKDSCG VGFVCHIKGQ
PNHQIVSDAR SLLCNMTHRG ATGADARDGD GAGVMTGIPH AFFLRESSLL SIELPAPGRY
AVGNVFFRPN PIEALIEHKA TFERIALTHK LKVLGWREVP RNNSILGPAA LSREPIILQP
IVVPDFNDPD ALFDEKEFER QLYVLRKHAS HTISLADWFY ICSLSNKVIV YKGQLSPSQV
YEYYYDLNHV LFQSHFCLVH SRFSTNTFPS WDRAQPLRWA AHNGEVNTVR GNKNWMKARE
GNLSSDKFGD QLDSLYPIIE EGGSDSAAFD NVLELLVVNG VLSLPEAIML LVPEAWQNNP
DMDPAKSAFY QWAACLMEPW DGPALFTFSD GRYCGANLDR NGLRPCRWVT TNEDIMICAS
EVGAITIAPE TITRKGRLQP GKMLLVDTHE GRIVDDKELK MTTAQKKPFR EWINNQLLRL
PDILEHNKSI SSTLLSDSLD TTRISEDPRL LAFGYTLEQL DLLMRPMVSD GKEALGSMGN
DAPLACLATQ ARLIYDYFRQ LFAQVTNPPI DPIRESIVMS LECYVGPEGN LLAMDESQAS
RLALPSPILS VQEFRALQDL HIFNPAWSSR TIDITFEKRS GLAGYVLTLD RICQAAGEAV
QAGCRLLALS DRAVSADRVA ISALAATGAV HHHLIKSKDR SKVALLVETG EAREVHHLCV
LLGYGADGIC PYLAMEAILK LRREGLVKGD LTDMDLIENF RHATNNGILK VMSKMGISTL
QSYKGAQIFE ALGLHQTVIE RCFVGTASRI QGTTFELLAL DAFEFHERGF PSRQIVLPPG
LPESGEYHWR DGGEAHINDP VSIANLQDAV RSKNQSAYDV YSQNAQKQVR AVTLRGLLDF
DYQSAQSIPL EQVEPWHELV KRFCTGAMSY GSISQEAHSA LAIAMNRLGG KSNTGEGGED
ASRSLVMPNG DTMRSAIKQV ASGRFGVTSN YLADSDELQI KMAQGAKPGE GGELPGHKVS
ESIAKTRHST AGVGLISPPP HHDIYSIEDL KQLIYDLKCA NPRARVSVKL VSEVGVGIVA
SGVAKAKADH ILISGHDGGT GASRWTGIKY AGLPWELGLA ETHQTLVLND LRGRVCLQTD
GQIRTGRDVA IAALLGAEEF GFATTPLIAM GCIMMRRCHQ NTCPVGVATQ DPVLRAKFTG
QPEHVINFFY YVAEELRTHM AKLGFRTLNE MVGRTDLLKV DETLRNPKTV NIDLSAVLKP
AWKMRPGVAT FKTKQQDHKM YTRLDNKFID EAEPAITKGL PVRIEADVKN TDRALGTSLA
NRVSKAYGEK GLERDTIHVD MRGSAGQSLG AFLASGITLE LEGDANDYVG KGLSGGRLIV
YPPRSSPFKA EENVIVGNVC LYGATSGEAY LRGIAAERFA VRNSGAIAVV EGVGDHGCEY
MTGGRVVVLG STGRNFAAGM SGGIAYVLDM ARDFKSKVNQ EMVELGTVND PHEIAGLRGM
IEDHRHFTKS EQAARILRKF NEFLPRFVRV MPLDYKAVLE AGSKAAMQSD PHKHIPGFDI
KGDAYNPVED KAKTNVNDQL EVPAATLAHP EPPVVDLEDA MVDEASAKQI VEKLDKTKGF
MKYKRLNENY RNPKSRTKDW AELSTRLTES QLKVQAARCM DCGVPFCQSD TGCPISNVIP
KWNDLVFKGQ WLDALNRLLM TNNFPEFTGR ICPAPCEGAC VLGINEAPVG IKSIECAIID
KGFEMGWIVP RPPPQRTGKK VAIIGSGPAG LACADQLNRA GHTVTVYDRN DRHGGLLMYG
IPNMKLDKKV VQRRLDLMTA EGVTFVANAH VGVSTDANEI RAANDALVVS TGATWPRNLN
LPNRNLDGIH FAMEFLQLNT KSLLDSELTD SSYLSAKGKN VIVIGGGDTG NDCIGTSLRH
GAKSVTNFEL LPQPPQSRAS DNPWPQWPKV FRVDYGHTEV QNFFGKDPRE YCISTKEFVS
DGNGKLKGLN TVRVEWTKDS RGAWKMKEVA GTEEFYECEL CLLALGFLGP EESMIKALGL
KQDGRSNIVT NVGENQRKFE YQTSLDGVFA AGDCRRGQSL VVWGIQEGRA AAVDVDNFLT
GNSASKLPSK GSIKLRHFAV DPSFEPVTTI SA
//
