ID   GLTB_PORYE              Reviewed;        1538 AA.
AC   Q1XDB2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase;
DE            EC=1.4.7.1;
DE   AltName: Full=Fd-GOGAT;
GN   Name=gltB;
OS   Porphyra yezoensis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51; TISSUE=Gametophyte;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP006715; BAE92499.1; -; Genomic_DNA.
DR   RefSeq; YP_537056.1; -.
DR   GeneID; 3978887; -.
DR   BRENDA; 1.4.7.1; 257472.
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_0000277304.
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;  168811 MW;  5993783A58126647 CRC64;
     MFNQKIVDQA PRKLTSRLTN SSSLISIEKE RDACGVGFIA DVNNVANHKI VVQALEALTC
     MEHRGACSAD RDSGDGAGIT TAIPWNLFQK SLQNQNIKFE QNDSVGVGML FLPAHKLKES
     KLIIETVLKE ENLEIIGWRL VPTVQEVLGK QAYLNKPHVE QVFCKSSNLS KDRLEQQLFL
     VRKKIEKYIG INGKDWAHEF YICSLSCYTI VYKGMMRSAV LGQFYQDLYH SEYTSSFAIY
     HRRFSTNTMP KWPLAQPMRF VSHNGEINTL LGNLNWMQSR EPLLQSKVWK DRIHELKPIT
     NKDNSDSANL DAAVELLIAS GRSPEEALMI LVPEAFQNQP DFANNTEISD FYEYYSGLQE
     PWDGPALVVF TNGKVIGATL DRNGLRPARY VITKDNLVIV SSESGVVQVE PGNVKSKGRL
     GPGQMISVDI FSHKILNNKE IKTSVTTKIP YGELLTDARQ ILEHKPFLSD QQVDIKKLMQ
     LQTAFGYTNE DVELVIEHMA SQAKEPTFCM GDDIPLSILS EKSHILYDYF KQRFAQVTNP
     AIDPLRESLV MSLAIQIGHK SNLLDDQPTL AKHIKLESPV INEGELNAIF ESKLSCIRIN
     TLFQLEDGPK NFKQQIQQLC ENASQAILDG NNILVLSDKN NSLDSEKVSI PPLLAVGAVH
     HHLINKGLRQ EASILVETAQ CWSTHHFACL IGYGASAICP YLAFETARHW WSNPKTKMLM
     SKGRLPACNI QEAQANYKKA VEAGLLKILS KMGISLLSSY HGAQIFEILG LGSEVVNLAF
     KGTTSQIGGL SMIELGRETV NIHSKAFSEV KTKKLANYGF VQYRPGGEYH INNPEMSKAL
     HQAVRGYNPE YYNNYQSLLQ NRPPTALRDL LKLQSNRAPI SIDEVESIED ILQKFCTGGM
     SLGALSRETH ETLAIAMNRI GGKSNSGEGG EDPVRFKILN DVNSSGTSPL LPHLKGLKNG
     DTASSAIKQI ASGRFGVTPE YLMNAKQLEI KIAQGAKPGE GGQLPGKKIS PYIATLRKCK
     PGVPLISPPP HHDIYSIEDL SQLIFDLHQI NPKAKISVKL VSEIGIGTIA AGVAKGNADI
     IQISGHDGGT GASPLSSIKH AGSPWELGLS EVHQLLAENQ LRDRVTLRVD GGLRTGSDIV
     LAAIMGAEEF GFGTVAMIAT GCIMARICHT NKCPVGVATQ REELRARFSG VPEALVNFFL
     FIGNEVREIL ASLGYKSLDD ITGQNHLLIK NTDINLTKTN GIQLDTLINI NNNTWTKFNS
     VHTNGPVMDD DILAIPEVSN AIKLETEITK HFKIANTNRT VGTRLSGIIA KNYGNTGFKG
     LIKLNFYGSA GQSFGAFLAS GINLKLMGEA NDYVGKGMNG GSIVIVPPAG TIYEDNNQVI
     IGNTCLYGAT GGYLFAQGQA GERFAVRNSL AESVVEGVGD HACEYMTGGV IVVLGKAGRN
     VGAGMTGGLA YFLDEDENFI DRVNSEIVKI QRVITKAGEE QLKNLIENHA AKTGSLKAHT
     ILEKWNSYLP QFWQVVPPSE ANIDETNPTY SSNTIAAC
//