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Database: UniProt
Entry: A0A1I3JG25_9FLAO
LinkDB: A0A1I3JG25_9FLAO
Original site: A0A1I3JG25_9FLAO 
ID   A0A1I3JG25_9FLAO        Unreviewed;      1498 AA.
AC   A0A1I3JG25;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:SFI59169.1};
GN   ORFNames=SAMN05443431_101395 {ECO:0000313|EMBL:SFI59169.1};
OS   Olleya namhaensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1144750 {ECO:0000313|EMBL:SFI59169.1, ECO:0000313|Proteomes:UP000199559};
RN   [1] {ECO:0000313|Proteomes:UP000199559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28881 {ECO:0000313|Proteomes:UP000199559};
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; FORM01000001; SFI59169.1; -; Genomic_DNA.
DR   STRING; 1144750.SAMN05443431_101395; -.
DR   Proteomes; UP000199559; 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; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
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:UP000199559}.
FT   DOMAIN          17..413
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1498 AA;  166950 MW;  2F14D045136DC1E7 CRC64;
     MLKKQGLYLP EFEHDNCGAG FICSLTGKRS NDIIHKALEI LVKLEHRGAV SSDGVTGDGA
     GILIDIPHKF FKIFCEFDLP EAGEYAVSNV FLPKKENQRQ YCIDVFEKEI QNQGLKLIGW
     RDVPVNSTVL GEIAKVTEPF VKQIFIGKAS DTQTEREFNI KLYAARKIAE HTIYDSKLSE
     SQFFYLPSLS TKIIIFKGLL MPEHINEYYL DLFNSALDTR LALVHQRFST NTFPTWDLAQ
     PFRYICHNGE INTVRGNVSR MFSREEIMES PLFGDDIKKI IPTILRGKSD SATLDMVVEL
     LLMTGRSLPE AMMMLVPEAW EKNPHMSDSK KAFYEYNSCL MEPWDGPASI PFTDGNFIGA
     VLDRNGLRPS RYTVTKQGNV IMSSETGVVD IAPENIEFHG RLEPGKMFLV NMSEGRIVND
     EEIKEEIAAK HPYRQWLNEN LIHLRDIEAK EGHIKYDEID LKKREVVFGY TEEDLNTIIR
     PMAQLGKEPI GSMGSDTPIA ILSERPQLIY NYFKQLFAQV TNPPLDGIRE ELITDISLTL
     GSDVNIFDIN AEHCKKLKIQ NPVISKHDLD KIRDYDTNPD FKVESISMLY EVNRGLNELE
     VALENLVTKA SKAIDEGANI IILSDRFVDE NHAPIPALLA CSYLNHALHK LEKRSKISLI
     IESAEPREVH HFALLFGYGA SAVNPYIVNE IVQQQINNAD LTDLEYLAAI KNYNKAVGKG
     ILKVMNKIGI STLNSYRGSQ LFECIGIKTS TVEKYFPNTP TRIQGIGLRE IEQEIVKRHK
     RAFHKNTEPQ IEVGGDYRWR RGQEKHMFNP LTVAKLQESV RTNKASTFKE FSDLVNDQSK
     SLMTIRGLFE FDQFDPIPLE EVEPWTEIVK RFKTGAMSYG SISKEAHENL AVAMNRIGGK
     SNSGEGGEDQ ERFYKSSQGD WRNSAIKQVA SGRFGVTSNY LTSASEIQIK IAQGAKPGEG
     GQLPGPKVNP EIAKTRNSTP YVGLISPPPH HDIYSIEDLS QLIYDVKSAN REARINVKLV
     SEIGVGTVAA GVAKAKADVI LIAGFDGGTG ATPLTSQKHT GLPWELGVAE AQQTLVMNDL
     RNRVVLECDG QLKTGRDVAI ACLLGAEEFG FATAPLVASG CIMMRVCHLN TCPVGIATQN
     PDLRKKFKGK PEHVVNYMYF VAQELREIMA KLGFRTINEM VGQSQKLNRN KAIDHYKSSG
     IDLTPILHKV EVAEDVQLYN TYCQDHNLNV HLDFKIIKQA HQALFRRQKT NLAMPITNID
     RAVGAVISNE ISKIYGADGL PEDTIDIDFT GSAGQSFGAF ATKGLKFTVH GNTNDYLGKG
     LSGAKLIIKV PEKCAIIPED NIITGNVTLY GATSGEVYIN GKAGERFCVR NSGAQAVVEG
     IGDHGCEYMT GGVAVILGTV GRNFGAGMSG GVAYVLDDKG TFKQNCNSED LNIDPIENEA
     DSLQLKQLIE NHFEATGSPL AARILKDWNN YLPKFKKVLP EEYRQALVRL EQEQLELA
//
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