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
//