ID A0A0N5CLR5_THECL Unreviewed; 1789 AA.
AC A0A0N5CLR5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=TCLT_LOCUS1063 {ECO:0000313|EMBL:VDM96299.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000106201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000106201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM96299.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYYF01000112; VDM96299.1; -; Genomic_DNA.
DR STRING; 103827.A0A0N5CLR5; -.
DR WBParaSite; TCLT_0000106201-mRNA-1; TCLT_0000106201-mRNA-1; TCLT_0000106201.
DR OMA; WDGPAAM; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; 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; 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 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; 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 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; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 2.
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; SSF51971; Nucleotide-binding domain; 2.
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:UP000276776}.
FT DOMAIN 106..389
FT /note="Glutamate synthase central-N"
FT /evidence="ECO:0000259|Pfam:PF04898"
FT DOMAIN 457..826
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
FT DOMAIN 910..1106
FT /note="Glutamate synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01493"
FT DOMAIN 1311..1419
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 1434..1607
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 1675..1759
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1789 AA; 198764 MW; AD22AAE68E9993DE CRC64;
MIELIDDRLR PGRILLVDTV EKKIEEDGDL KLRIALLRPH KKLNSARIYL DQLRRNDVLS
HGAITNEYLI KRELELQWNE ESCTSNTGKR ILKKCHRDFH LDEDRRLMAF SFSPDTFAML
IAPMIIEKKE ALGSMGNDAA LACLSDYSPQ ISSYFQQLFA QVTNPPIDPF REQIVMSLRC
PIGPESNLLE PMEELEGRLI LEQPVLSLVD LEVLKRTTYK NWRTIVIDAV YPTQHDSKGL
LPALDRICSE ACAAALDGYQ LIVLSDRKVC QKLVAIGPLL ALGAVHQCLL KQQLRMKVAL
IVESGQVKVV HDFCVLLGYG ADAICPYLVY ESCHRLRNMG LFDADINDEQ VFQGYKAGIE
RGIFKVMAKM GISTLHSYKG AQIFEAVGLA EEVVNRCFTN TVSRLGGATF EILAAEALRV
HRNAYPAASD KDYNYGDSKT LISPGIFHWR DGGERHINEP ANIAKLQAAT KLNDRKTFHE
YSVASNLAQR MCTLRGQLEI KTSKKFQIPL SEVEPASEIV KRFVTGAMSF GSISWETHTT
LAIAMNRIGG KSNTGEGGEK PERYRSDQPK DYNLRSAIKQ IASARFGVDS AYLANADELQ
IKMAQGAKPG EGGELPGHKV SVEIAATRRS TPGVGLISPP PHHDIYSIED LAQLIYDLRC
ANPLARISVK LVSEAGVGII AAGVAKGKAE HITVSGHDGG TGASSWTGIK HAGLPWELGI
AETHQVLCMN NLRSRVVLQA DGQIRTGRDV MIAALLGADE FGMSTAPLIV LGCTMMRKCH
LNTCPVGIAT QDPLLRAKFR GKPEHVVNFM FMVAEEVRYF LSKLGLRTLQ EAIGRVDLLY
ASPSPINKKA TMLEFGNILF NAQKLFPDYN FRGGSVKQII DISNLEKQVI ASVKELIDGH
SAHKHLKDLE IVNTDRAFGV RLSYYQISKQ CGEKGFSNDR SIRINLVGHA GQSFGAFLVK
GVSLYLEGDA NDYVGKGLSG GKIVIYPNRN VTFLSEKNSI IGNAALYGAT SGKYRIFFTP
LSGLVLFRGI AGERFAVRNS GAIAVIEGVG DHGCEYMTGG KVIILHSIGR NFAAAMSGGL
AFIHDGKRQW TRYINTATID LEEPDNEDLA WIKEMTDVFV QETGSKIGNA ILENWDNEYK
KFIKIFPKDY KRAIERMKET LKIAEEKESL KKNEYMLSRR IPPRQRKFSM DMQIAIGPVR
RKMAPGSEGD KQVLADSGKK YLKNVRIEDY TGFEEAKDSQ EVVEEEEDDD EPSDAGESEI
EDTNDLSVVD IENIPGLNGS KDNDKSLDKL RGFMKYRRQK VVYRPVEERI KSWKEITDYR
AVRSNIREQA ARCMDCGVPF CQGNTGCPLG NIIPKWNDYV FKQNWRQALE QLLQTNNFPE
FTGRVCPAPC ETACCLAINS PAVTIKSIEC AVIDYAFLQG WMEPHKPNYS TGKRIAIIGS
GPAGMAAAAQ LNKVGHAVVV YEKKNHAGGL LRYGIPTMKL DKYIVDRRVK LLEDEGVRFI
TNTEIGKHVP ADFLLRDNDA ILVCTGSTIP RDLSILNREA KGICFAMNFL EKSQRIVAGE
EDSWEGLDAK GKRVIILGGG DTATDCIATC TRLGAESVLA LEIMSRPPDE RYPDNPWPQW
PIIFRTDYGH EERKHITGDD PRLFALSTKK FLVNESTSGQ KVLTGLLTVE VEWKKDDNGN
WKMFEIENSE RELLCDLCIL AMGFVGPEKS VIEQLGLDTS IRSNILTGEE RYNTSKSKVY
AAGDCRRGQS LVVWAIHEGR QAARQIDYDL MGKTTLAGPG GVVLAPIQN
//
