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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//