ID A0A0M4NWW3_9GAMM Unreviewed; 1500 AA.
AC A0A0M4NWW3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:ALE52377.1};
GN ORFNames=SP60_03575 {ECO:0000313|EMBL:ALE52377.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52377.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE52377.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52377.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
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; CP010552; ALE52377.1; -; Genomic_DNA.
DR RefSeq; WP_053951320.1; NZ_CP010552.1.
DR STRING; 1705394.SP60_03575; -.
DR KEGG; tho:SP60_03575; -.
DR PATRIC; fig|1705394.5.peg.718; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000058020; Chromosome.
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:UP000058020}.
FT DOMAIN 24..425
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 907..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1500 AA; 164289 MW; 6C379A8883713B10 CRC64;
MKTPLLHLPK AHGLYSPNNE KENCGVGFIA HVKGQPSHQI TLDALEMLSR MDHRGGCGCE
ANTGDGAGIL TNIPHDFFTA EIQTLFGQTV AQGDYGVGNI FLPQDSTQRA HCMSLMEAAI
SNEGQVFIGW RDVPVDTQKA DVGDIARESQ PIIKQLIIGK AKGIDTKAFE RALFIIRKQT
SHTIRTDETL TEAMLFYVCS LSTSIIIYKG MLMGSQVLDF YSDLSNPEYS TYLAMVHSRF
STNTFPSWDR AQPCRYMSHN GEINTRQGNF NWMRAREGTL ESEFFADNLE KTLPVIETEV
SDSGSFDNVL EFLMMNGRTL QEAVLMMVPE AWQNDANMSD EKKAFYEYFS NVMEPWDGPA
SIAFTDGHQI GAVLDRNGLR PSRYYLTHDD RVIMASEVGV VDVATDNVKT KGRLRPGKMF
LVDFDKGVLI DDEAIKADFA AKNPYREWLN AQQIHLSDLG CEKEAHGFHP DSLIHRLQAF
GYSTETLQFM LLPLVNELRD PVGSMGNDSA LACLSDQSRI IYDYFKQLFA QVTNPAIDSI
REEVVMSLRC SIGPEGNLLA NNPKNAHRLV VDHPILTNEE TAALRHCNHL GWTSKTIDIT
YDINSGKKIS TLLDEICAKG SKAIKDGHSL IILSDRNIGS NRVAISSLLA SSALHRHLVS
SSERTQVGII VETGEAREVH HFCLMTGFGA DAINPYLAFE ALWQARRDNM IDADSDDAII
ASYRKGVAKG MLKVMAKMGI STLESYKGAQ IFEAVGLAPE IMDKCFFETA SRIDGVGFDI
LQAEGEKRHQ HAYKAISLDN KGQYHWRSGG EQHMWDPKTI SNLQLAARNN DESAYWAFAK
HANEEGTRNS TLRGLMSFKQ GKSISIDEVE PAQEIVKRFA TGAMSFGSIS AESHESLAIA
MNRLGGKSNT GEGGEDAKRW TPDANGDSRR SAIKQVASGR FGVTIDYLNN ADEIQIKVSQ
GAKPGEGGEL PGSKVDEGIA AIRHSTPGVG LISPPPHHDI YSIEDLSQLI FDLKRSNPEA
RISVKLVAEV GVGTIAAGVT KAKSDHIVIA GHDGGTGASP LTSIKHAGLP WELGLAETHQ
TLVMNDLRSR VVIQTDGQLK TGRDVAIGVL LGAEEFGFST APLITMGCIM MRKCHLNTCP
VGIATQDKAL RKKFTGKPEH VVNYLFMVAQ ELRLIMADLG FKTVNEMIGR VDMLEMNQAI
EHWKQGTINL DALLTPAQKP HANTSTYQTE VQDHQLELHL DNTLFEQSKA VIDGTKAVKI
TSKITNVDRA VGAMLSSRLV KARGGNTLAD DSVQVKFTGS AGQSLGAFTA KGITLEVEGD
ANDYVGKGLS GGKVIVYPPK NSTFNAEDEI IAGNVCGYGA TGGEIYLSGC VSERFCVRNS
GVTAVVEGIG DHGCEYMTGG RVAILGEVGR NFGAGMSGGI AYVYNPHDTF KDMVNPIMID
LDSMDAEAQT ELKSFISNHA QYTGSKVAQR ILDHWDEEIQ HFIKVMPKDY KRVLAENAEK
//
