ID   GLTB_HORVU              Reviewed;         436 AA.
AC   Q08258;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase;
DE            EC=1.4.7.1;
DE   AltName: Full=FD-GOGAT;
DE   Flags: Fragment;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-436, AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Maris Mink;
RX   MEDLINE=93237792; PubMed=7763576; DOI=10.1007/BF00198209;
RA   Avila C., Marquez A.J., Pajuelo P., Cannell M.E., Wallsgrove R.M.,
RA   Forde B.G.;
RT   "Cloning and sequence analysis of a cDNA for barley ferredoxin-
RT   dependent glutamate synthase and molecular analysis of
RT   photorespiratory mutants deficient in the enzyme.";
RL   Planta 189:475-483(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; S58774; AAC60547.1; -; mRNA.
DR   PIR; T06210; T06210.
DR   UniGene; Hv.25558; -.
DR   HSSP; P55038; 1LM1.
DR   Gramene; Q08258; -.
DR   BRENDA; 1.4.7.1; 283.
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; IPR000583; GATase_2.
DR   InterPro; IPR017932; GATase_II.
DR   Pfam; PF00310; GATase_2; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   3Fe-4S; Amino-acid biosynthesis; Chloroplast;
KW   Direct protein sequencing; FAD; Flavoprotein; FMN;
KW   Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Plastid.
FT   CHAIN         1   >436       Ferredoxin-dependent glutamate synthase.
FT                                /FTId=PRO_0000170795.
FT   DOMAIN        1    400       Glutamine amidotransferase type-2.
FT   ACT_SITE      1      1       For GATase activity (By similarity).
FT   NON_TER     436    436
SQ   SEQUENCE   436 AA;  48752 MW;  63E0C7CCD04400B6 CRC64;
     CGVGFVANLS NEPSFNVVRD ALTALGCMEH RGGCGADNDS GDGAGLMSGI PWDLFDDWAS
     KEGLVPFERT HTGVGMVFLP QNENSMEEAK AAVEKVFTDE GLEVLGWRPV PFNLSVAGRN
     AKETMPNILQ IFVRIAKEDD ADDIERELYI CRKLIERATK SASWADELYF CSLSSRTIIY
     KGMLRSEVLG QFYLDLQNEL YKSPFAIYHR RFSTNTSPRW PLAQPMRLLG HNGEINTIQG
     NLNWMRSREA TIQSPVWRGR ENELRPFGDP KASDSANLDN AAELLLRSGR SPAEAMMMLV
     PEAYKNHPTL SVKYPEVIDF YEYYKGQMEA WDGPALLLFS DGRTVGACLD RNGLRPARYW
     KTSDGFVYVA SEVGVIPMDE SKVVMKGRLG PGMMITVDLE TGQVLENTEV KKNVASAKPY
     GTWLQESTRS IKPVNF
//