ID   GLTB_ANTSP              Reviewed;        1536 AA.
AC   Q06434;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase;
DE            EC=1.4.7.1;
DE   AltName: Full=Fd-GOGAT;
GN   Name=gltB; Synonyms=glsF;
OS   Antithamnion sp.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Ceramiales; Ceramiaceae;
OC   Antithamnion.
OX   NCBI_TaxID=2767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94033299; PubMed=8219058; DOI=10.1007/BF00021421;
RA   Valentin K.-U., Kostrzewa M., Zetsche K.;
RT   "Glutamate synthase is plastid-encoded in a red alga: implications for
RT   the evolution of glutamate synthases.";
RL   Plant Mol. Biol. 23:77-85(1993).
CC   -!- CATALYTIC ACTIVITY: 2 L-glutamate + 2 oxidized ferredoxin = L-
CC       glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H(+).
CC   -!- COFACTOR: Binds 1 3Fe-4S cluster.
CC   -!- COFACTOR: FAD.
CC   -!- COFACTOR: FMN.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine
CC       (ferredoxin route): step 1/1.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
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DR   EMBL; Z21705; CAA79809.1; -; Genomic_DNA.
DR   PIR; S39510; S39510.
DR   HSSP; P55038; 1OFD.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IEA:EC.
DR   GO; GO:0005506; F:iron 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   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000583; GATase_2.
DR   InterPro; IPR017932; GATase_II.
DR   InterPro; IPR002932; Glu_synth_centr_C.
DR   InterPro; IPR006982; Glu_synth_centr_N.
DR   InterPro; IPR002489; Glu_synthase_C.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 2.
DR   Gene3D; G3DSA:2.160.20.60; Glu_synthase_C; 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   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   3Fe-4S; Amino-acid biosynthesis; Chloroplast; FAD; Flavoprotein; FMN;
KW   Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Plastid.
FT   CHAIN         1   1536       Ferredoxin-dependent glutamate synthase.
FT                                /FTId=PRO_0000170790.
FT   DOMAIN       27    427       Glutamine amidotransferase type-2.
FT   NP_BIND    1105   1162       FMN (By similarity).
FT   ACT_SITE     27     27       For GATase activity (By similarity).
FT   METAL      1158   1158       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1164   1164       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1169   1169       Iron-sulfur (3Fe-4S) (By similarity).
SQ   SEQUENCE   1536 AA;  171112 MW;  E803CED3004F321C CRC64;
     MQVSKYFTHQ LSQFSGYPSI VSERDACGVG FIANLNSKPS NKIVTEALNA LSCMEHRGGC
     GADNISGDGA GVTIQIPWDI FISEGINFLP KLQSNQSILN YGVRMILRSS DDLDKIKKIF
     SWALDEYQLD LISWRNVPVD KSILGEESKF NQPLVVQCIV RSNNLIDYKL DKHLYLVRKK
     IEKLVSKLDI NTNKQFYICS FSSKTIVYKG MLRSEFLVKY YNDLSNSLYV SNFAMYHRRF
     STNTMPKWSL AQPMRFMAHN GEINTLLGNL NWNKSKESLL KSSIWSDYYD ILSPITNLEN
     SDSANLDSVL ELFIHSGRTP QEALMILIPE AYKNQPALSL FPEITDFYEY YSILQEPWDG
     PALVVFTDGK FVGATLDRNG LRPARYTITD DGFISLSSET GVSNINSQNV VTKGRLGPGQ
     MLCVDLSKNL VLDNWMIKQQ ISQKFPYKEW VNKYQSNLNL LEYLNDFTFD KVQMNRWHTA
     FGYTNEDVEL VIEHMASSAK EPTFSMGDDT PLPILSEKPH LIYDYFKQRF AQVTNPAIDP
     LRESLVMSLI TYLGPKGNIL EPTAIMAKSI KLESPIINEN ELAQLNSFNL SVVTVPTFID
     KHLSTQTFVD KILEICSQCD SYISQGIEIL VLSDRIEILP VDKIFVSPLL IVGAVHHYLI
     KKQLRHKVSL VIDTGQCWTT HHFALLIGYG ASAICPYLAF LTVRQWWHNS RTQKLMSTGK
     LSRLTIQESQ DNYRSAIEKG LLKILSKMGI SLLSSYHGAQ IFEILGLGQD VVDLAFSGTV
     SRLNGMTLNE LYEDSLKSYN LAFITEIPKK LPNLGYVQYR PSAEYHVNNP EMSKTLHKAV
     RNNDNILYSK YKSLLNDRRP TNLRDLLELK TDRQPISIDQ VEDVNSVLMR FCTGGMSLGA
     LSRETHETLA IRMNRIGGKS NSGEGGEDST RFKSIQDLDT SGVSRTFSHL KGLKINDLAS
     SAIKQIASGR FGVTPEYLVN AKQLEIKIAQ GAKPGEGGQL PGKKVSPYIA ELRNCKPGVT
     LISPPPHHDI YSIEDLAQLI FDLHQINPDA QVSVKLVASL GIGTIAAGVA KGNADIIQIS
     GHDGGTGASP LSSIKHAGAP WDVGLAEVHT TLVENSLREK VILRVDGGLR TGKDIIIAAL
     MGAEEFGFGT VAMIATGCVM ARVCHTNNCP VGVATQRQDL RNRFPGIPSD VVNFFIFVAE
     EVREILAELG YKSLEELIGL NDLFKVKDIE LSKTKNLNLN ILFNSINMNR NLIPKLKHKT
     VHTNGNVLDD ILLSKSNIIN AINLQSNIVQ DIEILNTDRC VGARISGLIT KMYGRDNFNG
     NLQLNFVGSA GQSFGAFISK GIHLYLKGEA NDYVGKGMNG GEIIICPPIE QKTSSSNQVI
     LGNTCLYGAT GGYLFANGQA GERFAVRNSN GYSVVEGVGD HACEYMTGGL IVVLGTFGRN
     IGAGMTGGIA YFLDEDNTLK NKLNTEIVKA QRLLTKESEE QLKNIMELYE IKTKSEKAKL
     ILDNWSQYLA KFYQIVPPSE QIQHLLMLIF FFSKYC
//