ID A0A0P7ZK73_9CYAN Unreviewed; 1555 AA.
AC A0A0P7ZK73;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=glutamate synthase (ferredoxin) {ECO:0000256|ARBA:ARBA00039085};
DE EC=1.4.7.1 {ECO:0000256|ARBA:ARBA00039085};
GN ORFNames=HLUCCA11_12075 {ECO:0000313|EMBL:KPQ35150.1};
OS Phormidesmis priestleyi Ana.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ35150.1, ECO:0000313|Proteomes:UP000050465};
RN [1] {ECO:0000313|EMBL:KPQ35150.1, ECO:0000313|Proteomes:UP000050465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ana {ECO:0000313|EMBL:KPQ35150.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPQ35150.1}.
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; LJZR01000014; KPQ35150.1; -; Genomic_DNA.
DR STRING; 1666911.HLUCCA11_12075; -.
DR PATRIC; fig|1666911.3.peg.4488; -.
DR Proteomes; UP000050465; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:KPQ35150.1}.
FT DOMAIN 28..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1531..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1555 AA; 168573 MW; 5FA231D3C0BC01D3 CRC64;
MTLNPTTFQT DVLESLGPSW LVEERDACGV GFIADQKGRA SHRLVVDTLT ALDCMEHRGG
LCADQSSGDG AGIMTAIPWE LLQEWASESG IQAFTPQQTG VAMVFLPQQA SDLKVAQTLF
EQAVSATGLT FLGWREVPVA PETLGPLALK FQPQIAQALV TSAESKGDEL ERSLFLARRR
FEQLIAQKAK ETDSPALANA YVCSFSARTI VYKGMVKSAV LGQFYTDLQN EAYKSAFAIY
HRRFSTNTLP KWPLAHPMRL LGHNGEINTL IGNINWMSAR EANLAHPSWG EDLALLKPVV
NVENSDSANL DNVMELLVRT GRSPAQALTM MVPEAYNNQP ELADYPEIVD YYEYYSSIQE
PWDGPALIVF CDGKQVGATL DRNGLRPARY VITRDGYVIV SSEAGVVDIP VEDIVEKGRL
GPGQMLAVNF EDSHEILHNW EIKQRIAQAQ PYGQWLAERR VEISPQLFSE QTRLDEQTLL
TQQTAFGFTA EDVDMIIQDM AAQGKEPTFC MGNDTPLAVL SEKPHLLYDY FKQRFAQVTN
PPIDPLRERL VMSLSTQLGA QGNLLEEHPD QARLMKLESP VINDTEMAMI RKSDFPVSDI
STLYAVEGGP LGLEAAIKAL CDNAAKAVST GSQILILSDR ISSTGETTTL SGQQTYIPPL
VAVGAVHHHL IAQGLRMETS LIVDTAQCWS THHFACLLGY GATAICPYLA LESVRHWWAD
KKTQKQMETG KLPVSTLNGA QTNYRKAVEN GLLKILSKMG ISLLSSYRGA QIFEAVGIGT
DLREIAFKGS VSRLGGLSIS ELAQETMSFH QKAFPELTRK RLENMGFVQS RPSGEYHMNN
PAMTKLLHKA VETQQYDHYE VYREQLSGRP VAALRDLLDF KSDREAIALT EVESVESIMK
RFCTGGMSLG SLSREAHETL GIAMNRIGGK SNSGEGGEDA VRFEVLDDVD SNGFSATLPH
LKGLQNGDTA SSAIKQVASG RFGVTPEYLM SAQQIEIKMA QGAKPGEGGQ LPGKKVSEYI
ASLRNSKPGV TLISPPPHHD IYSIEDLAQL IFDLHQINPR AGVSVKLVAE VGIGTIAAGV
AKANADVIQI SGHDGGTGAS PLSSIKHAGL PWELGLTEVH RALMDNQLRD RVTLRVDGGL
KTGWDVIMGA LMGAEEYGFG SIAMIAEGCI MARVCHTNQC PVGVATQQEV LRKRFSGTPG
KVVNFFYFIA EEVRSLLAKL GYRSLDEIVG RADLLVARDD VSLTKTKALD LSSLVKLPDV
KSDRAWLTHG DIHSNGPVLD DDILADADVA AAIAQQGTVT KHWNVINTDR TVGARIAGAI
AQKYGNTGFS GQLNLTFKGS IGQSFGAFNI GGMRLTLVGE ANDYVGKGMN GGEIVIKPFE
QATYQAADNV IVGNTCLYGA TGGTLYASGI AGERFAVRNS KGKAVIEGAG DHCCEYMTGG
VVVVLGKVGR NVGAGMTGGL GYFLDEAGDF QTRVNPEIVQ VQRVLTAAGE QQLKSLIEAH
ANRTNSAKAK QILSDWPHYL SQFWQVVPPS EADSPEAGVQ GVQGVQKDKT ASTVV
//
