ID A0A218XKI4_PUNGR Unreviewed; 1645 AA.
AC A0A218XKI4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=glutamate synthase (ferredoxin) {ECO:0000256|ARBA:ARBA00039085};
DE EC=1.4.7.1 {ECO:0000256|ARBA:ARBA00039085};
GN ORFNames=CDL15_Pgr019097 {ECO:0000313|EMBL:OWM85473.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM85473.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037928}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWM85473.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MTKT01001276; OWM85473.1; -; Genomic_DNA.
DR UniPathway; UPA00045; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal 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 CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF1; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE 1, CHLOROPLASTIC_MITOCHONDRIAL; 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 SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 112..511
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1645 AA; 178914 MW; D0856DA96B1DBAD5 CRC64;
MASVPQLLHS NALSAKSCSV LLSDRGKASG LLLVDFVGLY CKSKHTSRRR QLGLSTSRAF
PHFAAKSLPT PVRAVLDLDR TASSLDDSSA SQSGPKPQVA NLEDILSERG ACGVGFIANL
DNKASHQIIK DALVALGCME HRGGCGADND SGDGSGVMTL IPWDLFNSWV TEQGISSFDK
LHTGVGMVFL PKDADLLDEA KKAIVNIFQQ EGLEVLGWRP VPVDTSVVGY YARETMPNIQ
QVFVRVVKED SIADVERELY ICRKLIEKAA SSASWGEDLY ICSLSNQTIV YKGMLRSEVL
GLFYLDLQKD LYRSPFAIYH RRYSTNTSPR WPLAQPMRFL GHNGEINTIQ GNLNWMQSRE
TSLKSPVWRG RENEIRPFGN PKASDSANLD SAAELLIRSG RAPEEALMIL VPEAYKNHPT
LMIKYPEVVE FYEYYKGQME TWDGPALLLF SDGKTVGACL DRNGLRPARY WKTSDNVVYV
ASEVGVLPMD ESKVTMKGRL GPGMMITVDL SSGQVYENTE VKKRVALSNP YGKWITENMR
TLKPVNFLSA TMMENESILR HQQAFGYSSE DVQMVIESMA AQGKEPTFCM GDDAPLAVLS
QKSHMLYDYF KQRFAQVTNP AIDPLREGLV MSLEVNLGKR GNILEVGPEN ASQVSLSSPV
LNEGQLEALL KDPILKAQVL PTFFDIRKGV EGSLQRTLNR LCEAADEAVR NGAQLLVLSD
RADELEPTRP AVPILLAVGA VHQHLIENGL RMSASIVADT AQCFSTHQFA CLIGYGASAV
CPYLALETCR QWRLSNKTVN LMRNGKMPTV TIEQAQKNFV KAVQAGLLKI LSKMGISLLS
SYCGAQIFEI YGLGKDIVDL AFCGSVSKMG GLTFDELARE TLSFWVKAFS EDTAKRLENF
GFIQFRPGGE YHGNNPEMSK LLHKAVRQKS MSAFSVYQQH LANRPVNVLR DLLEFRSDRA
AIPVGKVEPA TSIVERFCTG GMSLGAISRE THEAIAIAMN RLGGKSNSGE GGEDPIRWSP
LTDVVDGYSP TLPHLKGLQN GDTATSAIKQ VASGRFGVTP TFLVNADQLE IKIAQGAKPG
EGGQLPGTKV SAYIARLRNS KPGVPLISPP PHHDIYSIED LAQLIFDLHQ VNPNAKVSVK
LVAEAGIGTV ASGVAKGNAD IIQISGHDGG TGASPISSIK HAGGPWELGL TETHQTLIEN
GLRERVVLRV DGGFKSGVDV MMAAAMGADE YGFGSIAMIA TGCVMARICH TNNCPVGVAS
QREELRARFP GVPGDLVNYF LYVAEEVRGM LAQLGYEKLD DVIGRTDLLK PRDISLVKTQ
HLDLSYLLSN AGMPKWSSTE IRKQVVHTNG PVLDDVILAD PELVYVLIKL AIPYTLPVQI
SDAIENEKVI HKTLQIYNVD RAVCGRIAGV VAKRYGDTGF AGQLNITFTG SAGQSFACFL
TPGMNIRLVG EANDYVGKGM AGGELVVTPV DETGFCPEEA TIVGNTCLYG ATGGQVFVRG
KAGERFAVRN SLAQAVVEGT GDHCCEYMTG GCVVVLGKVG RNVAAGMTGG LAYILDDDDT
LIPKVNKEIV KIQRVTAPVG QMQLKSLIEA HVEKTGSTKG AKILQEWDKY LPLFWQFVPP
SEEDTPEACA EYQTTDADQV TLQSA
//
