ID   GLTB_CYACA              Reviewed;        1549 AA.
AC   O19906;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase;
DE            EC=1.4.7.1;
DE   AltName: Full=Fd-GOGAT;
GN   Name=gltB;
OS   Cyanidium caldarium.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   MEDLINE=20496959; PubMed=11040290;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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 (By similarity).
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; AF022186; AAB82683.1; -; Genomic_DNA.
DR   PIR; T11974; T11974.
DR   RefSeq; NP_045078.1; -.
DR   HSSP; P55038; 1OFD.
DR   GeneID; 800212; -.
DR   BRENDA; 1.4.7.1; 145.
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   1549       Ferredoxin-dependent glutamate synthase.
FT                                /FTId=PRO_0000170791.
FT   DOMAIN       37    435       Glutamine amidotransferase type-2.
FT   NP_BIND    1116   1173       FMN (By similarity).
FT   ACT_SITE     37     37       For GATase activity (By similarity).
FT   METAL      1169   1169       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1175   1175       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1180   1180       Iron-sulfur (3Fe-4S) (By similarity).
SQ   SEQUENCE   1549 AA;  172012 MW;  6C0965E071453CB4 CRC64;
     MISISKRTSI ARINLSEFHT ISKIDRYPWL NKEKDACGVG FIAHLDNKFG HKLMMNALEA
     LATMEHRGAC SADEESGDGA GILFSIPWKF FVEWSLRYKQ FKINISQAAV AMLFLPCLSS
     DIQVSKNIVE EIFQDEDFIV IGWREVPYVK EVLGPLALRN MPQIYQIVVQ SKRYQGRSLD
     FHLYRVRRKI EKEITVRAYS WAKDFYFCSC SNHTIVYKGM VKSTSLGQFY QDLYNPDFEI
     SFAVFHRRFS TNTMPRWPLA QPMRILGHNG EINTLLGNLK WMEARESSLN HPTLNEVASI
     GPVVNVSNSD SANLDSVVEL FLHVGHSCPE ALMFLIPEAY ENNPKLKYHQ NLISFYEYCA
     GFQEAWDGPA LIVFSDGHTV GASLDRNGLR PARYCVTEDN VLILASEGGV LNLDPSLIRL
     KGRLGPGEMI VLDLQEKLLM SNLEIKNKIA SLRPYSDWIK QNRQVLIPTS FLTSTTLPLQ
     EVFKRQTCFG YTSEDIELVI ENMAIQGKEP TFCMGDDTPL AVLSGKSHVL YDYFKQRFAQ
     VTNPPIDSLR ESLVMSISSY LGSKTNSFEE SSEKILKIKT PILSENDLVL IKNSELLTET
     LVTTFEAHFD SPQANGQSLF STINQLCKQA KNLIQAGTKI IILSDKVCFE SRTESYIPPL
     LVVGSLHQYL IKQGVRQKVS LIVETGQCWS THHFACLLGY GASAVCPYLA LETVRHWWMS
     ERTQNLMSKG KMPNLTLIEV QNNYCKSVER GLLKILSKMG ISLLTSYIGA QIFEILGLGK
     EVVDLAFEGT VSRIGGLSFA DLAMETIDLC SAGFSKLNKK KLDNHGFVQY RPGGEYHLNN
     PEMSKALHKA VRENNYTLYE AYKQLLANRP PTNIRDLLEF NFRSCSVPLE KVENIFEITK
     RFCTGGMSLG ALSREAHETL SIAMNRIGGK SNSGEGGEDS LRFTVLTDVD ETGNSPSFPH
     LKGLKNGDSL SSAIKQIASG RFGVTPEYLV NAKQLEIKIS QGAKPGEGGQ LPGKKVSPYI
     ATLRACKPGV TLISPPPHHD IYSIEDLAQL IFDLHQVNPE CKVSVKLVSE IGVGTIAVGV
     AKAGAEIIQI SGHDGGTGAS PLSSIKHAGV PWELGLHEVH CLLVENNLRE KVILRVDGGL
     RTGQDVVMAA LLGADEYGFG TIAMIAGGCI MARVCHTNSC PVGVATQKEE LRMRYPGVPE
     NVVNYFIFLA EEIRVILSKL GFETLSQIIG RKDLINHNFD KKLCKTHCID TSIFFNIKTN
     EYNFLEIPGG HSKKLKTSLL DYELLNSSDI LYAIDNHKTL EKHIKISNSD RSVGAKLAGR
     LAKQYKNEGF RGSLILNFYG TAGQSFGSFN IKGVTLRLIG EANDYVGKSM SGGEIVIVPP
     SEVAFDASEQ VILGNTCLYG ATGGFLFAYG AAGERFAVRN SNAFSVLEGV GDHACEYMTG
     GRVVVLGKAG RNIAAGMTGG IAYFLDEYSN LPEKVNLDIV RIQRVVTNEA RKQLIQLIEK
     HVLKTGSKKA VLILQQWEIF IHYFWQIVPP SESETSETNY FVENKVLAN
//