ID A0A1H3D4J5_9EURY Unreviewed; 1542 AA.
AC A0A1H3D4J5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SDX61331.1};
GN ORFNames=SAMN04487946_101360 {ECO:0000313|EMBL:SDX61331.1};
OS Halobellus clavatus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=660517 {ECO:0000313|EMBL:SDX61331.1, ECO:0000313|Proteomes:UP000199170};
RN [1] {ECO:0000313|Proteomes:UP000199170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10118 {ECO:0000313|Proteomes:UP000199170};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; FNPB01000001; SDX61331.1; -; Genomic_DNA.
DR STRING; 660517.SAMN04487946_101360; -.
DR Proteomes; UP000199170; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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; 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; 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; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 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 SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000199170}.
FT DOMAIN 53..447
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1542 AA; 167850 MW; 18E795A932C26121 CRC64;
MAHITLYVVS EPLCLQEKML YGAVTREPMT KPHKHTTGES VGLADPTDER SNCGVGAVID
LDGGRSHETV ADGLELLENL EHRGTTGAEQ NTGDGAGIMV QRPDEFFDAV VDTELPDQYA
VGSIFMPQDD AAREGLIAIF ERILSEHGLN VRHWRDVPTD NSDLGATALE SEPDVWQAFV
VPNGDLSDDE FDRALYVARR AVENEVEELD SAGAARFYIC SLSRKTLVYK GLLKGDQLAE
YYLDLADERL ETTLTLVHAR FSTNTLGAWH LAHPYRHIIH NGEINTIQGN INWMRSRETD
LEHPDFGEDL ETLKPVINDP DQSDTASVDN AVELLLQGGR DLPHVLRMLI PEAYRGDDRM
DEDRRDWYDY HASLLEPWDG PALVAATDGD RVAAVLDRNG LRPCRYDVTT DNTLVMASEV
GALDTDPSEI ETRGRLQPGQ LFVADPDEGR VIPDEEVFES LTDEKYGEWV ETEQRQLDEL
ADSDEYAPRD EIEHLRAAQA AFGYTHDQLS HLIEPMAEDG KDPVGSMGDD TPLSVLSDFN
RPLFTYFKQL FAQVTNPPLD YIREELVTSL ESRLGAQQNL LDESPEHARQ LVLDSPVLTD
AQTAGIKSLG DRDSDQMKST IVDISYERGT DLEAAVERVR DDAAAAIEDG ANVIVLSDRN
AGPDRVAIPS LLVTGAVHHS LVRNGYRNHA GLVLESGDPR EVHHLATLVG YGADAVNPYL
AYQTIADVVA GPDGADESEA IAAYKKALED GLLKTMAKMG ISTVESYQGA QIFEAVGLDS
DFVAEYFEGT EIRTEGIGID VIEEDVLTRH TVAYGDDPQL DRQGEYEHRS DGIHHQWNPQ
TVGTLQQAVR SGDYEKYQEF AELINDQSEE LQTLRGLLEF DSDRESVPVE EVEPVADIVE
RFSTAAMSLG SLSPEAHENN SIAMNRLGGK SNTGEGGEPP ERFGTEKECN VKQVASGRFG
VTSEYLTNAE EIQIKMAQGS KPGEGGHLPG KKVNEMIAHV RFATPGVGLI SPPPLHDIYS
IEDLKQLIHD LKAANPDADI NVKLVSEAGI GTIAAGVAKA NADVVHISGH DGGTGASPKT
SIKNAGLPWE LGLAEANQML RATDLRSRIR VTVDGGMKTG RDVAVGALLG AEEYVFGTAS
LVTSGCVMAR QCHENTCPVG VATQRENLRN RFPGQPDHVI NYMTFIAQEL REIMADLGFT
SLDEMIGRPS LLTQRETDHE KARHLDLSDV IAEPAGDSRR KTEEQIHAGV EAQLDHELIE
RAESALESGE PVAIDSDISN VDRAVGAMLS NRISKAHGNE GLPDDTIHCT FDGIAGQSFG
AFLASGVTMD LTGAANDYLG KGLSGGRIVV ETPENAAYEA DENVLIGNVA LYGATQGELY
VNGVAGERFA VRNSGVKAVV EGVGDHGCEY MTGGVVAVLG DTGRNFAAGM SGGIAYVYDP
DDEFESKTNT GMVSLSTELD DSDLQMLRRL IENHAGYTDS TRAQWMLDDW SEVVDDFVKV
MPDAYAEVIE ERARDDVRKE LPPAATAVAG DDSPTAAQTS DD
//
