ID F0RDU6_CELLC Unreviewed; 1503 AA.
AC F0RDU6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ADY29857.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:ADY29857.1};
GN OrderedLocusNames=Celly_2035 {ECO:0000313|EMBL:ADY29857.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29857.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY29857.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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; CP002534; ADY29857.1; -; Genomic_DNA.
DR RefSeq; WP_013621602.1; NC_015167.1.
DR STRING; 867900.Celly_2035; -.
DR MEROPS; C44.003; -.
DR KEGG; cly:Celly_2035; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_10; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016041; F:glutamate synthase (ferredoxin) 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; 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 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:ADY29857.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487}.
FT DOMAIN 18..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1503 AA; 167294 MW; 199E509036377751 CRC64;
MKLKKQGLYL PDFEHDNCGA GFICSLKGKK SNDIIHKALE ILDKLEHRGA VSSDGKTGDG
AGILIDIPHD YFTEVCDFNL PEPGEYAVAN IFLPQKQNQR DFCISVFEEN IKKQGLKLLG
WRDAPVNKNV PGRIAMETEP FVKQIFIAKE DSSQDYATFN LKLYIARKVT EHTILSSKLS
ESGFFYVPSL STKIIIFKGL LMPQDIKFYF KDLMDPRVVT RLALVHQRFS TNTFPTWDLA
QPFRYMCHNG EINTLRGNVS RMRSREELLK SDLFGDEIKN ILPIILPGKS DSATMDMVVE
LLLMTGRSLP EVMMIMVPEA WEKNPDMSPA KRAFYEYNSC MMEPWDGPAS VPFTDGNYIG
AVLDRNGLRP SRYSVTKDGY VIMSSETGVV DIEPENIEFH GRLEPGKMFL VNMEEGRIVN
DEEIKEKIAQ LKPYQKWLDN NLVHLKDIPY NDCPLFLGEE SLEKRKSLFG YTLEDINTII
LPMGKTAKEP IGSMGSDTPI AVLSEKPQLI YNYFKQLFAQ VTNPPLDGIR EELITDISLT
LGSDHNIFDF SELHCRKLKI QNPVISKEDL DKIKNYDASP DYKVTSIPIL YKIARGHNAL
EEALASILDQ ASKAIDNGTN IIILSDRNVD KDNAPIPALL ALSFVNSGLQ KLGKRSKLSI
IIESAEPREV HHFALLFGYG ASAVNPYLVN EIIAEQIEEN DITDITFDEA IKNYNKGIGK
GVLKVMNKIG ISTLNSYRGS QLFECIGINT KVVDKYFPNT PTRIQGIGLY QIEKEISKRH
QKAFNTKEVA ASLELEMGGA YRWRRDGEKH LFNPLTIAKL QKSVRNNEPE TYKEYSKLIN
EQSKHLMTIR GLFEFSNYDP IPIEEVEPWT DIVKRFKTGA MSYGSISKEA HENLAIAMNR
IGGKSNSGEG GEDAERFYKN ETGDWKNSAI KQVASGRFGV TSNYLSSAKE IQIKMAQGAK
PGEGGQLPGP KVNPSIAKTR NSTPYVGLIS PPPHHDIYSI EDLSQLIYDL KSANREARIN
VKLVSEVGVG TVAAGVAKAK ADVILVSGHD GGTGASPLTS LKHAGLPWEL GIAEAQQTLV
MNDLRNRVVV ECDGQLKTGR DVAIACLLGA EEFGFATAPL VASGCIMMRV CHLNTCPVGI
ATQNPELRKK FKGKPEHVVN YMYFIAQELR EIMAQLGFRT VNEMVGQVQK LDRKKAIEHY
KAEGIDLTPI LHQVSVPKET KLYNTQKQEH DIYKSIEFKI IEKAHPSLFR KEKLTLDFPI
KNTDRAVGAI ISNEISKTYG AKGLPINTLR LNFTGSAGQS FGAFATRGLT MTVNGNTNDY
LGKGLSGGKL VIKVPEGATI IPEENVITGN VTLYGATAGR AYINGKAGER FCVRNSGAKT
VVEGIGDHGC EYMTGGVAVI LGEVGRNFGA GMSGGIAYVL DPNKTFEKNC NKESLNLLPV
EEANDIAELK DLIESHYNYT MSPLAQRLLE NWENSLPMFV KVFPEEYRQA LKRLEEEQKA
SII
//
