ID B6HQ85_PENRW Unreviewed; 2122 AA.
AC B6HQ85;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=Pc22g11310 {ECO:0000313|EMBL:CAP98419.1}, PCH_Pc22g11310
GN {ECO:0000313|EMBL:CAP98419.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP98419.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP98419.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920437; CAP98419.1; -; Genomic_DNA.
DR RefSeq; XP_002565078.1; XM_002565032.1.
DR STRING; 500485.B6HQ85; -.
DR GeneID; 8307325; -.
DR KEGG; pcs:Pc22g11310; -.
DR VEuPathDB; FungiDB:PCH_Pc22g11310; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR OMA; WDGPAAM; -.
DR OrthoDB; 20503at2759; -.
DR BioCyc; PCHR:PC22G11310-MONOMER; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000000724; Contig Pc00c22.
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:UP000000724}.
FT DOMAIN 53..462
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 960..980
FT /note="Disordered"
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 2122 AA; 233582 MW; 26B93AD29D900B55 CRC64;
MGLNLEELYG KDISEEQAPH EYSQYQPEKG YGWANALPER QGLYDPEYEK DACGVGFAAH
IKGKPSHKIV SDARNLLCNM THRGAVGSDA RDGDGAGVMT SIPHKFFIKN FAREVGVDLP
PLGQYAVGNL FFKPDEEALK QSIVDFEELA TTLGLRVLGW REVPRDSTIL GPAALSREPI
VMQPFVVLKS AYGEGNKPEI TDTEKFDERT FELQLYVLRK RATHVIGLGN WFYLCSLSNR
NIVYKGQLSP VQVYTYYHDL VNVDYEGHFA LVHSRFSTNT FPSWDRAQPL RWAAHNGEIN
TLRGNKNWMR AREGVLRSEV FGDELDKLYP IVEDGGSDSA AFDNVLELLM INGVLSLPEA
VMIMIPEAWQ DNPAMDPAKS AFYEWAACQM EPWDGPALFT FSDGRYCGAN LDRNGLRPCR
FYVMDDDRIV CASEVGAIDI DPERVVQKGR LQPGKMLLVD TVAGRIIDDA ELKQTVARRQ
DFAGWLDKGL LQLPAINKLL LDSNVDLSFA LDNNTIQNDP RLRVFGYSFE QVSLILGPMA
ADSKEALGSM GNDAPLACIA LQPRLLYEYF RQLFAQVTNP PIDPIREAVV MSLECYVGPQ
GNLLEMDPSQ CHRLRLPSPI LSIPEFNALK NINIAHNDWT VRTIDITFEK SKGTAGYIEA
LDSICDGATE AIQNGDKVII LSDRATSADR VPVSALLATG LVHHHLVRNK WRSLAALAVE
TAEAREVHHH CVLLGYGADA INPYLALECI LKMNRENLIR KDIPDEKVVQ NYKSSCDGGI
LKVMSKMGIS TLQSYKGAQI FEALGIDDSV IDRCFSGTAS RIRGITFDLI AQDAFAFHER
GYPSRPIVEV PGLPESGEYH WRDGGEAHIN DPTSIANVQD AVRTKNDKSY EAYAKSAHEQ
IKNCTLRGML DFDFDQRTPI PIDQVEPWTE IVRRFVTGAM SYGSISMESH STLAIAMNRL
GGKSNTGEGG EDAERSKRME NGDTMRSAIK QIASGRFGVT SNYLADADEL QIKMAQGAKP
GEGGELPGHK VVGPIARTRF STPGVGLISP PPHHDIYSIE DLKQLIYDLK CSNPRSRVSV
KLVSEVGVGI VASGVAKAKA DHILISGHDG GTGASRWTGI KYAGLPWELG LAETHQTLVL
NDLRGRVVVQ TDGQIRTGRD LAIACLLGAE EYGFATTPLI ALGCIMMRKC HLNTCPVGIA
TQDPELRQKF KGTPEHVINF FYYVANEMRA IMARLGIRSV NEMVGRAELL KVRDDIRNVK
QERIDLSLIL TPAHSLRPGV ATYNVRKQDH RLHTRLDNKL IAESELALEK GLPCRIECDI
VNTDRALGAT LSYQISRRYG EAGLPQDTIH ANIKGSAGQS FGAFLAPGVT LELEGDANDY
VGKGLSGGRL IVYPSRGAAF KAEENVIVGN TCLYGATRGT CYFRGMAAER FAVRNSGATV
VVEGVGDHGC EYMTGGRVLN LGPTGRNFAA GMSGGIAYVL DKNQDFHSKV NLEMVEISSI
EDPSEIAFVR GLVEDHHHYT GSELAARILL DFTRALPHFV KVLPTDYKRV MEEEAAKAEA
AKKAEFTLPQ LPSIPVKAER AEADHSKKTD LLDIEDSISD SKAEKKRSAL ILDKTRGFMK
YSRRSEKYRN ATTRTRDWGE ISHRLSEDEL KYQSARCMDC GVPFCQSDTG CPISNIIPKW
NELVFSNSWQ DALNRLLMTN NFPEFTGRVC PAPCEGSCVL GINEDPVGIK SIECAIIDRG
FEMGWMVPCP PKTRSGKIVA IIGSGPAGLA AADQLNRAGH SVTVYERADR MGGLLMYGIP
NMKLDKKVVQ RRIDLMAAEG IKFVAGTAVG PDCEVSLQSL RATNDAVIVA TGATVARDLK
VTGRELDGVH FAMQFLHKNT KSLLDSGLSD GEYISAKDKH VVVIGGGDTG NDCIGTSVRH
GAKSVTNFEL LPQPPPERAR DNPWPQWPRI YRVDYGHTEV KTHMGKDPRE YCVMSTEFVD
DGNNRVKGIN TVRVEWTKSA TGGWDMKTLE GSEQFFPADL VLLSMGFLGP EDRVFGDEIE
LDPRKNIKTP PGHYSTNIPG VYAAGDCRRG QSLIVWGINE GRQCAREVDT FLSGTSSQLP
VTGGIVRRPA IDSVPQPTEV AA
//
