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Database: UniProt
Entry: M1XS44_NATM8
LinkDB: M1XS44_NATM8
Original site: M1XS44_NATM8 
ID   M1XS44_NATM8            Unreviewed;      1507 AA.
AC   M1XS44;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:CCQ37130.1};
DE            EC=1.4.-.- {ECO:0000313|EMBL:CCQ37130.1};
GN   Name=gltB {ECO:0000313|EMBL:CCQ37130.1};
GN   OrderedLocusNames=Nmlp_2987 {ECO:0000313|EMBL:CCQ37130.1};
OS   Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS   8.8.11).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ37130.1, ECO:0000313|Proteomes:UP000011867};
RN   [1] {ECO:0000313|EMBL:CCQ37130.1, ECO:0000313|Proteomes:UP000011867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC   {ECO:0000313|Proteomes:UP000011867};
RX   PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA   Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA   Gross K., Schuster S.C., Oesterhelt D.;
RT   "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT   of a previously haloalkaliphilic genus.";
RL   Genome Announc. 1:e0009513-e0009513(2013).
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; HF582854; CCQ37130.1; -; Genomic_DNA.
DR   RefSeq; WP_015409880.1; NC_020388.1.
DR   STRING; 268739.Nmlp_2987; -.
DR   GeneID; 14651637; -.
DR   KEGG; nmo:Nmlp_2987; -.
DR   eggNOG; arCOG04553; Archaea.
DR   HOGENOM; CLU_000422_8_2_2; -.
DR   OrthoDB; 211693at2157; -.
DR   Proteomes; UP000011867; Chromosome.
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   ECO:0000313|EMBL:CCQ37130.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011867}.
FT   DOMAIN          24..418
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          894..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1478..1507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1507 AA;  164605 MW;  2745ECC9758F449F CRC64;
     MSEPIDRSAT ADGLADPGDY RANCGVGVVM DLDGERSHGT VADGVELLEN LEHRGTTGAD
     ENTGDGAGIL LQTPHEFFDD EIPELPDAGE YAVGAVFMPP NEEAIARLQD LAEHVFAEHG
     LDVFAWRDVP TDNALLGETA VESEPVVVQC FVRSDLDDDA FDRALYVARR DLETTVEERT
     FEGAARFYIC SLDRETVVYK GLLTAEQLPS YYPDLLDDRV RSTFAMVHAR FSTNTLGAWH
     LSHPYRNIIH NGEFNTIQGN INWMRAREDD LQHPDFGDDI ETLRPIINDP EQSDTASVDN
     ALELLMAGDR EMPHALRMLI PEAWRGEANR VSEDRREWYD YHASLVEPWD GPALVAATDG
     TRIGAVLDRN GLRPCRYDVT TDNTLVMASE AGALEYDFGE IERRDRLQPG QLFVADPEEG
     RVVPDEEIFD DLVEEKYGEW VDERQVALDD IADADESAPR DPVDSIRSQQ ALYGYTEDEM
     NHLIEPMATD GKDPVGSMGD DTPLSVLSQF NRPLFTYFKQ LFAQVTNPPL DYIREELVTS
     METRLGYQRN LLDETPAHAE QLVADSPVLT DAQTGAIKGL DGDLSSAVVD ITFDPEDDLE
     TAVRDVRREA TIAAQEHDIV VLSDRNAGPD AIPIPALLAT GGVHHHLVRN GLRNHVGIVL
     ESGDPRAVHH VATCIGYGAG AVNPYLAFQS IADIVAGPDG ADEERAIEAY IGAVEDGLLK
     TMAKMGISTV ESYQGAQIFE AVGLDSDFVA EYFEGTTART EGADIDDIDA DLRKRYEVAF
     ADDPRLELQG EYEHRSSGMF HEWNPQSVGT LQKAVRSGDY GEYLEFAEQM NDQTENLQTL
     RGLLEFDSDR DPVDIEDVEP VEEIVERFST AAMSLGSISP EAHENNCIAM NRLGGKSNTG
     EGGEPPERFG TEKECSVKQV ASGRFGVTST YLTNADEIQI KMAQGSKPGE GGHLPGEKVN
     EMIAHVRYST PGVGLISPPP LHDIYSIEDL KQLIHDLKAA NPEADINVKL VSEAGIGTIA
     AGVAKANADV VHISGHSGGT GASPKTSIKN AGLPWELGLA EANQMLRSTD LRSRIKVTVD
     GGMKTGHDVA VGALLGAEEY VFGTASLVTS GCVMARQCHE NTCPVGVATQ REDLRKRFPG
     EPQHVINYMT FIAQELREIM ADLGFESVEE MIGRVDALEQ RDDVEQERAR KLDLSAVLAE
     PAGDQRYKTE PQTHEIDDAL DWDLIEEAEA AIESGEPVHI DRDISTVNRA VGATLSNEIS
     KRHGTDGLPE DTVRIDFGGT AGQSFGAFLQ DGVTMGLTGT ANDYVGKGLS GGRLVLNTPN
     DAPYEPEENI LVGNVALYGA TQGEAYINGM AGERFGVRNS GVKAVVESVG DHGCEYMTGG
     VVACLGRTGK NFAAGMSGGV AYVLDRDGDF EETVNYGMVS TTDELDHRDR TMLRRLVENH
     VAHTDSDRGE YILDNWEEEL TKFVKVMPDA YADIIDEREE ADVRTDLPES VTPTADSERP
     GHVASDD
//
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