ID K9X609_9NOST Unreviewed; 1570 AA.
AC K9X609;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=glutamate synthase (ferredoxin) {ECO:0000256|ARBA:ARBA00039085};
DE EC=1.4.7.1 {ECO:0000256|ARBA:ARBA00039085};
GN ORFNames=Cylst_5006 {ECO:0000313|EMBL:AFZ27057.1};
OS Cylindrospermum stagnale PCC 7417.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Cylindrospermum.
OX NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ27057.1, ECO:0000313|Proteomes:UP000010475};
RN [1] {ECO:0000313|EMBL:AFZ27057.1, ECO:0000313|Proteomes:UP000010475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ27057.1,
RC ECO:0000313|Proteomes:UP000010475};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037928}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; CP003642; AFZ27057.1; -; Genomic_DNA.
DR RefSeq; WP_015210292.1; NC_019757.1.
DR STRING; 56107.Cylst_5006; -.
DR KEGG; csg:Cylst_5006; -.
DR PATRIC; fig|56107.3.peg.5498; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_3; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000010475; Chromosome.
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; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF1; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE 1, CHLOROPLASTIC_MITOCHONDRIAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000010475}.
FT DOMAIN 36..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1549..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1570 AA; 170641 MW; 209640B5BEDB7A50 CRC64;
MTNKPMNQGQ NITLSDIHAR DTYPGQRWLA EERDACGVGF IAQRQNYASH SIVNKALVAL
TCLEHRGGCS ADQDSGDGAG ILTAIPWELF QHNSALSSID FSSTSSLAVG MIFLPQDPEA
AQKAKATVEQ LAAEEKLTVL GWRVVPVQPD LLGVQARENQ PQIEQVFLTS ADQSGDELER
KLYITRSRII KAAKNISEEF YVCSLSSRTI VYKGMVRSAV LGEFYLDLKN PAYKSAFAVY
HRRFSTNTMP KWPLAQPMRL LGHNGEINTL LGNINWMMAR EASLNHPVWG DRINELKPLV
HIDNSDSATL DNVLELLVRS GRSPLEALMI MVPEAYQNQP SLANYPEIVD FYEYYSGLQE
AWDGPALLVF SDGQKVGATL DRNGLRPARY VITKDDYIVV ASEAGVVDFP EANILEKGRL
GPGQMIAVDL ATNEVLKNWQ IKQRIAKKHP YGEWLQQHRQ ELKQLVRGGS VVNGNGNGNG
NGNGHSPTDN VELTTDKIDK HSLLQQQTAF GYNTEDVEMV IQPMASTGSE ATFCMGDDIP
LAVLSEKPHL LYDYFKQRFA QVTNPAIDPL REKLVMSLKV ELGERGNLLE PKPEYARKLK
LESPVITEAE LSAIALSGFA TAELSTLFAI SAGPEGLKAA VESLQAQAAE SVRAGAKILI
LSDRVGEGIG TEYTYIPPLL AVGAVHHHLI REGLRMKTSL IVKTAQCWST HHFGCLLGYG
AGAVCPYLAL ETVRDWWSDP KTQQFMARGK ITALTLEQAI ANYRQAVESG LLKILSKMGI
SLLSSYQAAQ IFEAIGIGGD LLALGFQGTT SRLGGLSVSE LAQEVLSFHS KAFPELTSKK
LENLGFVQYR PGGEYHMNSP ELAKALHKAV DGKKYDHYEV YKQHLKGRPV TALRDLLDFR
GDRQSIPLEE VESVSDIVKR FCTGGMSLGA LSREAHETLA IAMNRIGGKS NSGEGGEDPV
RYKVLNDVDE FGHSPTLPHL KGLRNGDTAS SAIKQVASGR FGVTPGYLAS AQQIEIKIAQ
GAKPGEGGQL PGPKVSPYIA MLRRSKPGVT LISPPPHHDI YSIEDLAQLI FDLHQINPKA
QVSVKLVAEI GIGTIAAGVA KANADIIQIS GHDGGTGASP LSSIKHAGSP WELGLSEVHR
VLMENSLRDR VILRVDGGLK SGWDVLIAAL MGGEEFGFGS IAMIAEGCIM ARICHTNNCP
VGVASQKEEL RKRFTGMPEH VVNFFYFIAE EVRSLLARLG YRSLSEVIGR ADLLTVRQDV
HLTKTQSLNL DCLIQLPNSQ ENRSWLVHET VHSNGPVLDD QILADAEIQA TIRNQSTVSK
TFPIVNTDRT VGSRLAGAIA SHYGDSGFEG QINLNFHGSA GQSFGAFNLP GLTLTLVGEA
NDYVGKGMHG GEIIIKPPAD ATYNPAQNVI VGNTCLYGAT GGVLFANGLA GERFAVRNSK
GVAVIEGAGD HCCEYMTGGV IVVLGKVGRN VAAGMTGGLG YFLDEDGLFP ELVNRSIVKT
QRVITEAGSK QLYELIKTHS DRTGSPKAKL ILQNWQEFLP KFWQLVPPSE AESPEANPEA
ETETKLLSSV
//
