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Database: UniProt
Entry: A5FHX7_FLAJ1
LinkDB: A5FHX7_FLAJ1
Original site: A5FHX7_FLAJ1 
ID   A5FHX7_FLAJ1            Unreviewed;      1519 AA.
AC   A5FHX7;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:ABQ05189.1};
DE            EC=1.4.1.14 {ECO:0000313|EMBL:ABQ05189.1};
GN   OrderedLocusNames=Fjoh_2161 {ECO:0000313|EMBL:ABQ05189.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05189.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ05189.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ05189.1; -; Genomic_DNA.
DR   STRING; 376686.Fjoh_2161; -.
DR   MEROPS; C44.003; -.
DR   KEGG; fjo:Fjoh_2161; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_10; -.
DR   OMA; TVFRLQH; -.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:ABQ05189.1}.
FT   DOMAIN          38..428
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          914..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1519 AA;  168854 MW;  64994530D7F7C303 CRC64;
     MFNEIFIFVK KISRMRVKEQ GLYLPEFEHD NCGAGFICNL NGIKSNDIIH KALDILIKLE
     HRGAVSSDGR TGDGAGILFD IPHDFFKKVC DFEIPEAREY AVGMVFLPKS KNQVSFCINA
     FEATIKDQNL KVLGWRDVPV DVENLGEIAA EKEPTVKQVF VSKNGQDLTE QEFNAKLFAA
     RKIAEHAVRG SKTSESHMFY FTSLSTTTII YKGLLMPEDI SRYYIDLKDP DLVTRLALVH
     QRFSTNTFPS WDLAQPFRYM CHNGEINTLR GNVSRMRARE ELMQSKVFGD DIKKLFPIIL
     EGKSDSASMD MVVELLLMTG RSLPEAMMMV VPEAWEKHQT MSPEKRAFYE YNACIMEPWD
     GPASIPFTDG NVIGALLDRN GLRPSRYTLT KSGFVIMSSE IGVLDIDPED VIQHGRLEPG
     KMFLVDMNEG RIIEDEEVKK AIVTKRPYQQ WVDENLLPLA SVPYTNNPTP VEKLDFLTRQ
     RLFGYTIEDL KTIINPMGSD GAEAISSMGN DTPLAVLSDQ PQLLYNYFKQ LFAQVTNPPL
     DGIREEIITD ISLAIGGDFN IFEIESKQCK KLKIQNPVVS NEDLDKIRNI DHPDFKSATI
     STLYKIEKGV NGLERALEKC VQATFKAVEE GCNIIILSDR GVSEELAPIP MLLACSYIHH
     SLNILQVRSK FGIIIESAEP REPHHFALLF GYGASAINPY MVNEIIHDQV EKGFITKVKA
     DYAVVNYNKA IAKGIVKIMN KIGISTLHSY RAAQIFEILG LNKTFTSKYF PYTPSRIEGI
     GLMEVEKEVK KRFQKAFPNS KIANLLSLEI GGIYRWRRGG EKHMFNPTTI SKLQQAVRLN
     SPESYKEYSN AVNEQSSNLM TIRGLFEFNN LDPISIDEVE PWTEIVKKFK TGAMSYGSIS
     REAHENLAIA MNRIGGKSNS GEGGEDPKRF QKEINGDSRN SAIKQVASGR FGVSINYLTN
     AKEIQIKMAQ GAKPGEGGQL PGEKVVPWIA ETRNSTPYVG LISPPPHHDI YSIEDLSQLI
     YDLKNANREA RINVKLVSEV GVGTIAAGVA KAKADVILIS GYDGGTGAAP LTSLQHTGIP
     WELGLAEAQQ TLILNDLRSR VVLECDGQLK TGRDVAIAAL LGAEEFGFAT APLVASGCIM
     MRACHLNTCP VGIATQDPEL RKNFKGTPEH VINFMYFIAE ELREIMAQLG FRTLKEMVGQ
     SQKLNVNKAI KHYKANGLDL SSILYKPEKA KTQPNHNTTT QDHQLENVLD FDIIKEAIPS
     IYRKEKTRVT FKIKNTDRSV GAILSNEISK IYGAQGLPDD TILVDFEGSA GQSFGAFATN
     GLSFKIHGNC NDYLGKGLSG GKLIVKVPPT ATFNPEDNII IGNVALYGAI TGEAYINGMA
     GERFCVRNSG ATAVVEGIGD HGCEYMTGGT VVVLGKTGRN FAAGMSGGVA YVYDPNKKFD
     STVCNMEMVA FDPMEEEDLT KLRKLIKNHS LYTSSPLAKR ILADWENQQQ HFVKVMPTDY
     KKALQRIAEE KKIEELIAG
//
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