ID A0A0A6PE47_9GAMM Unreviewed; 1495 AA.
AC A0A0A6PE47;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KHD08577.1};
GN ORFNames=PN36_19155 {ECO:0000313|EMBL:KHD08577.1};
OS Candidatus Thiomargarita nelsonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiomargarita.
OX NCBI_TaxID=1003181 {ECO:0000313|EMBL:KHD08577.1, ECO:0000313|Proteomes:UP000030428};
RN [1] {ECO:0000313|EMBL:KHD08577.1, ECO:0000313|Proteomes:UP000030428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hydrate Ridge {ECO:0000313|EMBL:KHD08577.1};
RX PubMed=27199933; DOI=10.3389/fmicb.2016.00603;
RA Flood B.E., Fliss P., Jones D.S., Dick G.J., Jain S., Kaster A.K.,
RA Winkel M., Mussmann M., Bailey J.;
RT "Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita
RT nelsonii Reveals Genomic Plasticity.";
RL Front. Microbiol. 7:603-603(2016).
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}.
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:KHD08577.1}.
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DR EMBL; JSZA02000078; KHD08577.1; -; Genomic_DNA.
DR Proteomes; UP000030428; 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: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 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:UP000030428}.
FT DOMAIN 20..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 905..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1495 AA; 165152 MW; E4ADFECDF5FCBC07 CRC64;
MGALPPKQGL YDPSNEHDAC GVGFIVHIKG HKNHEIINQG LEILKNITHR GAVGADPLAG
DGAGILIQTP DAFLRQAFAT LLPPLGEYGV GMIFLPRDDD IRADCEKIIT KVIANEGQSL
LGWRNVPTNN EGLSESVKGI EPVIRQVFIA NNCADQDAFE RKLFVIRKVI EHRVRDQLNI
DYADFYIPSL SSRTLLYKGM LLANQVGKYY PDLQDERMVT ALALVHQRFS TNTFPTWDLA
QPFRMICHNG EINTLRGNLN WMAARRYTMS SKLLGDDLDK LWPLIAEGQS DSACFDNALE
LLVAAGYSLG QAMMLLIPEA WTNNPLMDEK RRAFYEYHAA LMEPWDGPAA VGFTDGRQIG
ATLDRNGLRP ARYLITNDDL VVMASEMGVL DIPKAKIVKK WRLQPGKMFL IDTEQGRIID
DAELKAQLAK RAPYQDWLDQ TQIILEKLPP EVTAMPPNQE TLLDRQQAFG YTQEDLKLFL
IPMVVSGQEP IGSMGTDASL AVLSNRSRLL YDYFKQNFAQ VTNPPIDPIR EELVMSLVSL
IGPRPNLLGL NKEDLQKRLE VHQPILTNTD LEKVRRIEYR TEGAFRTKTL NMCYMAELGA
VCMEGALAEL CHQAEKAVLA GNNILILSDR ALDADNIAIP ALLATSAVHH HLIRKGLRTK
SGLVVETGEA REVQHFCLLA GYGAEAINPY LAFDTLFTIQ LPEKISQEEI EKRYIKAVNK
GILKVMSKMG ISTYQSYCGA QIFDALGLSD EFIEAYFTGT KCQTSGVGLT KIAEETVRRH
RMAFGNAPLY RNALDVGGEF AYRLRGENHI WTAETISKLQ HATRSNNRAL YDEFAREINE
QNERLLTLRG LFDFKFAEQS IPLSEVEPAS EIVKRFATGA MSFGSISYET HTTLAIAMNR
LGAKSNTGEG GEESERFKPL PNGDSKRSAI KQVASGRFGV TTEYLVNADD IQIKIAQGAK
PGEGGQLPGY KVDKTIARVR HSTPGVGLIS PPPHHDIYSI EDLAQLIHDL KNVNPQARIS
VKLVSEIGVG TVAAGVSKAH ADHITIAGYD GGTGASPMTS IKHAGSPWEV GLAETHQTLV
LNKLRGRTAV QTDGGLRTGR DVVIAAMLGA DEFGFATGAL IVAGCIMMRK CHLNTCPVGV
ATQDPKLRKL FSGQAAHIVN YFMFIAEEAR EWMAKLGFRT VNEMIGRSDK LEMRRALSHW
KAKGLDFSRI LYQPTLGPDV AVYNCEKQDH GLEKALDQAL IKQAKPALEQ RQAVRMSMQI
HNYNRTFGAM LSGEVAKRYG HAGLPEDTIY IKVTGCAGQS FGAFVARGVT IELEGEANDY
VGKGLSGGRL IIYPPKECPI VAEENIIVGN TVLYGAISGE CFFRGVAGER FAVRNSGAIA
VIEGVGDHGC EYMTGGVVVV LGVTGRNFAA GMSGGIAYVL DDTGEFEQRC NLSMVELEPV
DDALRLKTLI EKHWHYTNSR RAREILDNWS DYLPRFVKIM PVDYRRALQE TDKKP
//
