ID   GLTB_PORPU              Reviewed;        1538 AA.
AC   P51375;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase;
DE            EC=1.4.7.1;
DE   AltName: Full=Fd-GOGAT;
GN   Name=gltB;
OS   Porphyra purpurea.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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 (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
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; U38804; AAC08261.1; -; Genomic_DNA.
DR   PIR; S73296; S73296.
DR   RefSeq; NP_053985.1; -.
DR   HSSP; P55038; 1OFD.
DR   GeneID; 810015; -.
DR   BRENDA; 1.4.7.1; 279956.
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   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   1538       Ferredoxin-dependent glutamate synthase.
FT                                /FTId=PRO_0000170792.
FT   DOMAIN       34    431       Glutamine amidotransferase type-2.
FT   NP_BIND    1109   1166       FMN (By similarity).
FT   ACT_SITE     34     34       For GATase activity (By similarity).
FT   METAL      1162   1162       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1168   1168       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1173   1173       Iron-sulfur (3Fe-4S) (By similarity).
SQ   SEQUENCE   1538 AA;  168711 MW;  3F647CDB2F5C77CF CRC64;
     MFNQKIIEQA SGKLTGSLTK SSSLVSIEKE RDACGVGFIA DVNNIANHKI VVQALEALTC
     MEHRGACSAD RDSGDGAGIT TAIPWNLFQS GLKDKGIIIQ KNESIGVGML FLPTSKLQES
     KKIIENVLKE ENLEVVGWRL VPTVEEVLGK QAYLNKPHVE QMFCRSSNLS KNELEQQLFL
     VRKKIERYIG INGKEWAHEF YVCSLSCYTI VYKGMMRSAV LGQFYQDLYH SEYTSSFAIY
     HRRFSTNTMP KWPLAQPMRF ISHNGEINTL LGNLNWMRSR EPLLKSPIWK NRIDELKPIT
     NKDNSDSANL DAAVELLIAS GRSAEEALMI LVPEAFQNQP EFNKNTEISD FYEYYSGLQE
     PWDGPALVVF TDGKVIGATL DRNGLRPARY VITKDNLVIV SSESGVVQVE PSNIKSKGRL
     GPGQMISVDI ISHKILNNKE IKTSVAGKTP YGDLLKESRQ ILGHQAFFSE QQVESKKLMQ
     LQTAFGYTNE DVELVIEHMA SQGKEPTFCM GDDIPLAILS EKSHILYDYF KQRFAQVTNP
     AIDPLRESLV MSLTIQIGHK SNLLDDQPVL AKHIKLDSPI INEGELNAIL ESKLSCAHIN
     TIFKVEKGPN DFKKQIEQLC ESASQAILSG NNILILSDKN DILESEKVSI PPLLAAGAVH
     HHLINKGLRQ DASIIIETAQ CWSTHHFACL IGYGASAICP YLAFETARHW WSNPKTKMLM
     SKGRLPACNI QEAQANYKKA VEAGLLKILS KMGISLLSSY HGAQIFEILG LGSEVVNFAF
     KGTTSQIGGL SMEELGQETV NIHSKAFSQV KTKKLANYGF VQYRPGGEYH INNPEMSKAL
     HQAVRGYNPE YYNSYQRLLQ NRPPTALRDL LKLKSNKQPI AIDKVESMEN ILHKFCTGGM
     SLGALSRETH ETLAIAMNRI GGKSNSGEGG EDPVRFKVLN DVNESGNSDL LPHLKGLRNG
     DTASSAIKQI ASGRFGVTPE YLMNAKQLEI KIAQGAKPGE GGQLPGKKIS PYIATLRKCK
     PGVPLISPPP HHDIYSIEDL SQLIFDLHQI NPTAKISVKL VSEIGIGTIA AGVAKGNADI
     IQISGHDGGT GASPLSSIKH AGSPWELGLS EVHQLLAENQ LRDRVTLRVD GGLRTGSDIV
     LAAIMGAEEF GFGTIAMIAT GCIMARICHT NKCPVGVATQ REELRARFSG VPEALVNFFL
     FIGNEVREIL ASLGYKSLDE ITGQNHLLIK NTDIELAKTR GIELNSLINI NTHTWTKFNS
     VHTNGPVMDD DILAIPEIND AIKLENEVAK HFKIANTNRT VGTRLSGVIA QKYGNEGFKG
     LIKLNFYGSA GQSFGAFLAS GVNLKLMGEA NDYVGKGMNG GSIIIVPPAG TTYEDNNQVI
     IGNTCLYGAT GGYLFAQGQA GERFAVRNSL AKSVVEGVGD HACEYMTGGT IVVLGKAGRN
     VGAGMTGGLA YFLDEENKFI ERVNSEIVKV QRVITKAGEQ QLKNLIENHS AKTGSLKAHN
     ILENWNTYLP QFWQVVPPSE ANIEETNTAY SSNTITAY
//