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}.
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; 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
//