ID   GLTB_SPIOL              Reviewed;        1517 AA.
AC   Q43155; O81234;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 3.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase, chloroplastic;
DE            EC=1.4.7.1;
DE   AltName: Full=Fd-GOGAT;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Amaranthaceae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Melody; TISSUE=Leaf;
RA   Dincturk H.B., Knaff D.B.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 36-1517, AND PROTEIN SEQUENCE OF 1-24.
RC   TISSUE=Leaf;
RX   MEDLINE=94114561; PubMed=8286406; DOI=10.1016/0005-2728(94)90086-8;
RA   Nalbantoglu B., Hirasawa M., Moomaw C., Nguyen H., Knaff D.B.,
RA   Allen R.;
RT   "Cloning and sequencing of the gene encoding spinach ferredoxin-
RT   dependent glutamate synthase.";
RL   Biochim. Biophys. Acta 1183:557-561(1994).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- TISSUE SPECIFICITY: Leaves.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
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DR   EMBL; AF061515; AAC26853.1; -; mRNA.
DR   EMBL; U03006; AAA18948.1; -; mRNA.
DR   PIR; S67496; S67496.
DR   HSSP; P55038; 1OFD.
DR   BRENDA; 1.4.7.1; 286.
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   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   1517       Ferredoxin-dependent glutamate synthase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000170796.
FT   DOMAIN        1    400       Glutamine amidotransferase type-2.
FT   NP_BIND    1079   1136       FMN (By similarity).
FT   ACT_SITE      1      1       For GATase activity (By similarity).
FT   METAL      1132   1132       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1138   1138       Iron-sulfur (3Fe-4S) (By similarity).
FT   METAL      1143   1143       Iron-sulfur (3Fe-4S) (By similarity).
SQ   SEQUENCE   1517 AA;  165402 MW;  2304650E1F9350A6 CRC64;
     CGVGFIANLD NKGSFQIVKD ALTALGCMEH RGGCGSDNDS GDGSGVMTAI PWDLFNDWGK
     DQGIGPFDRS HTGVGMVFLP KDDLLAEEAK KVVLDTFAQE GIEVIGWRSV PTNVSVVGRN
     AKETMPNIQQ VFVRIIKEDS TDDIERELYI CRKLIERAAS SHTWASELYF CSLSNQTIIY
     KGMLRSEVLG MFYYDLQNER YTSPFAIYHR RYSTNTSPRW PLAQPMRFLG HNGEINTIQG
     NLNWMRSREP SIQSPVWRGR ENEIRPYGNP KASDSANLDS AAELLIRSGR TPEEALMILV
     PEAYKNHPTL MIKYPEAVDF YDYYKGQMET WDGPALLLFS DGKTVGACLD RNGLAPARYW
     RTVDNVVYVA SEVGVLPMDE SKVTMKGRLG PGMMISVDLS SGQVYENTEV KKRVASSNPY
     GKWVKENLRS LKAVNFLSRA LLENDTILRN QQAFGYSSED VQMVIESMAS QGKEPTFCMG
     DDIPLAVMSQ KPHMLYDYFK QRFAQVTNPA IDPLREGLVM SLEVNIGKRG NILEVGPENA
     SQVILPSPVL NEGELEALVN DPLLKAQMLP IFFDIRKGVE GTLEKRLNRL CEAADEAVRN
     GSQMLVLSDR SEELEPTRPA IPILLAVGAV HQHLIQNGLR MYTSIVVDTA QCFSTHQFAC
     LIGYGASAIC PYLALETCRQ WRLSNKTVNL MRTGKIPTVT IEQAQNNFCK AVKSGLLKIL
     SKMGISLLSS YCGAQIFEIY GLGKDVVDIA FQGSVSKMGG LTLDELARET LSFWVKAFSE
     DTAKRLENFG FIQFRPGGEY HVNNPEMSKL LHKAVRNKSE SAYAVYQQHL ANRPVSVLRD
     LLEFKSDRAP ISVGKVEPAT SIVERFCTGG MSLGAISRET HEAIAIAMNR LGGKSNSGEG
     GEDPIRWRPL TDVVDGYSST LPHLKGLQNG DTATSAIKQV ASGRFGVTPT FLVNADQIEI
     KIAQGAKPGE GGQLPGKKVS AYIARLRNSK PGVPLISPPP HHDIYSIEDL AQLIYDLHQI
     NPKAKVSVKL VAEAGIGTVA SGVAKGNADI IQVSGHDGGT GASPISSIKH AGGPWELGLS
     ETHQTLISNG LRERVILRVD GGLKCGVDVM MAAAMGADEY GFGSLAMIAT GCVMARICHT
     NNCPVGVASQ REELRARFPG VPGDLVNFFL YVAEEVRGIL AQLGFEKLDD IIGRTDILKP
     RDISLMKTQH LDLSYILASA GLPTMSSTAI RKQEVHTNGP VLDDQILSDP EIIDAIENEK
     IVNKTVKIFN VDRAVCGRIA GVIAKKYGDT GFAGQLNLTF EGSAGQSFAV FLTPGMNIRL
     VGESNDYVGK GMAGGELIVT PAENPGFRPE DATIVGNTCL YGATGGQIFV RGKAGERFAV
     RNSLAEAVVE GTGDHCCEYM TGGCVVILGK VGRNVAAGMT GGLAYILDED DTLIPKVNKE
     IVKIQRVTAP VGQMQLKNLI EAHVEKTGSS KGASILKDWD KYLPLFWQLV PPSEEDTPEA
     SAMFEQMTSE GASLQSA
//