ID A0A0D2X225_CAPO3 Unreviewed; 2366 AA.
AC A0A0D2X225;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=CAOG_002901 {ECO:0000313|EMBL:KJE91819.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91819.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) 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 -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; KE346363; KJE91819.1; -; Genomic_DNA.
DR STRING; 595528.A0A0D2X225; -.
DR EnsemblProtists; KJE91819; KJE91819; CAOG_002901.
DR eggNOG; KOG0399; Eukaryota.
DR InParanoid; A0A0D2X225; -.
DR PhylomeDB; A0A0D2X225; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000008743; Unassembled WGS sequence.
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 Gene3D; 3.20.20.70; Aldolase class I; 3.
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; 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:SF2; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE, CHLOROPLASTIC-LIKE; 1.
DR PANTHER; PTHR43100; 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 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; 2.
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};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743}.
FT DOMAIN 71..479
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2366 AA; 254066 MW; B8B59A5775CF5654 CRC64;
MLRAVFSTCS TARGLPSSML LKRRGYKTYQ PPSRASTLAQ QQQQPSPGNN AFTRFPAAQG
LYQPELEKDS CGVGMIVNIK GNPSHDIVKH GREVLVNMTH RGAVGAEENS GDGAGILASI
PHKLYARALE VQGVTLPPLG QYATGMVFLS ANPDVRQATK RALEERAASS GLAVLAWRDI
ATDNSSLGSV AKSAEPGISQ LFVVPNEAPN IPVAEATLRR RAFRFMREAR KGLAASAPLY
FCSLNTRTIV YKGQLTPEQL FPYFPEDLSD PLFSSHVVIV HSRFSTNTFP SWERAQPLRY
IGHNGEINTL KGNSNWMRAR EGVMSSPHFA ALDSLYPVIE PNGSDSQALD NSLEFLLNCS
DRSLPETMMM LVPEAWENMH SSANGITTSG STAARRHFYE WASHVSEPWD GPALFTFTDG
RFAGATLDRN GLRPSRFLVT KDDLLVMASE IGVVEGIPSN SIIKKGRLEP GRMLLVDTLE
GKIVNDHELK EKVATSRPYG KWIKGAVRLL PLVEKAEQLR SQSEHDNFSG AWASLPGSTA
FKGETASSSK LVRPSQAVRS ILLPLFGYTQ ETVSMLLAPM GEHGKEALGS MGNDAPLAVL
SRFPKLPSEY FKQLFAQVTN PPIDPIREAV VMSLRCAVGP SGNILETSAQ QCHRLVLDSP
ILTDAQLDAI KHVEQLDPST GFATRVFPLE YAFAAVEEGY SFIVLSDRGF VAKTEAALSA
NPASAHSSRF EQAAPISALL AVGAVHQHLL RSRQRLKVAL IVETAEAREV HHHCLMVGFG
ADAVCPYLAL DVIRSLSHKH TIRPDVHGRA NSTHVSQSDY NYIKSVNAGM LKVMAKMGIS
TLQSFKGAQI FEAIGLGQSV IDLCFTGTTS AVGGIGFAEI AYDTEERHRL AQVLLQQHRE
QQSVVQGLPT ELPYLSSSLS SHSLQGLSFK APTTSAAAVR LFSTTAARAR ANQHHLHLLA
STKAAGAATL TQDAPAAADE LATSVGQQPL HQTPHSVKDR HPVVPVTAGS LLSASLANRG
DYHWRANGEA HINDPESIAF LQDAARRNNT DAFARYTEYA NAAVRGCTLR GVIDIVGVDT
PASSESSGSA AVPLEEVESA ASILTRFCTG AMSYGSISEE AHTTLAIAMN RIGGKSNTGE
GGEDRKRYAS DPSAAASSAS SSTPQADSMR SAIKQIASGR FGVTIDYLYN SDEIQIKMAQ
GAKPGEGGEL PGHKVTGNIA ATRHSTPGVG LISPPPHHDI YSIEDLSQLI SDMKCANPKA
RISVKLVSET GVGIVASGVA KGKADHILVS GHDGGTGAST WTGVKSAGLP WELGLAETHQ
TLVLNGLRGR VVLQTDGQLR TARDVVVAAL LGAEEFGFAT VPLIALGCTM MRKCHLNTCP
VGIATQDPVL RAKFAGKPEH VVNFFFMLAE DIRGIMSKLG VRKFDELVGR SDWLAQRAAD
PLQPEQFAAK LQSIDLKGLL TPAFTLRPNV PTRFTTPQQH DALEATKLEN RLLSENEALK
QLLTGPAAPS VGTALTVETT IKNIDRTFGT LLSYHATAKF GAAGLPSNDA LVLQLHGSAG
QSLAAFLAPG ITVKLFGDSN DYVGKGLSGG IVVVRPPLDM PAEFKSDENV IVGNVCLYGA
TSGRAFFAGV AAERFAVRNS GALAVCEGVG DHGCEYMTGG RVVILGQTGI NFAAGMSGGI
AYVLDRDNEF SSHRCNREMV LLERVAAGSS DETELLELIR EHVTRTDSAV AKAILSDWES
IRPKFVKVFP HDYKRVLEQQ KQQKQQQQQQ QLQQPAASKQ APAFDAAPRR FFSMAAARRS
GANSTIKPTS SSFTSAKPLD KLRGFVTVER EEVGYRNEAD RVHDWEEVLH PTHVEGKTTA
SERAQTKAAA TPVVVATASS DEHLAKQTSR CMDCGVPFCQ SKSHGCPIGN LIPQFNELVF
QGNWREAYLQ LSTTNNFPEF TGRACPAPCE GACVVGIIDK PVTIKNVENA IIDHAFEQGW
VQPIIPMHRT GKRVAVVGSG PAGLAAADQL NRAGHSVTVY ERSDRFGGLL MYGIPNMKLD
KRAVQRRIEL LRASGVVFVP NTAVGTSQAV DDLAKEFDAV LLCTGSTVPR DLPVPGRNGR
GVHFAMDYLE PSTRALLGDF ESSGHKVPAE YDAHGKNVVV IGGGDTGADC IATAIRQGAR
SVVQFEINLQ PSKDGRAAAN PWPQYPKVFK VDYAHGEAAA VFQKDPREYV VLSTAFAVDP
SSKRVTGVHT NRLAWDVPAH THESIAGSEH TFPADLVLLA MGYQGPESEF AVAAGVQLNS
RGNFATALPQ PGLGIDVSYR THANKIYAAG DCRRGQSLIV WAINEGRMAA REIDLDLMGR
TLLPVTGGVT LASTSQLAPQ RIAARG
//
