ID H6MRR7_GORPV Unreviewed; 1527 AA.
AC H6MRR7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Ferredoxin-dependent glutamate synthase 1 {ECO:0000313|EMBL:AFA73723.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:AFA73723.1};
GN Name=gltB3 {ECO:0000313|EMBL:AFA73723.1};
GN OrderedLocusNames=GPOL_c27020 {ECO:0000313|EMBL:AFA73723.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73723.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA73723.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; CP003119; AFA73723.1; -; Genomic_DNA.
DR STRING; 1112204.GPOL_c27020; -.
DR MEROPS; C44.003; -.
DR KEGG; gpo:GPOL_c27020; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR Proteomes; UP000009154; Chromosome.
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:SF133; GLUTAMATE SYNTHASE (NADH); 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:AFA73723.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT DOMAIN 26..432
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1527 AA; 165431 MW; F10BEE0B58EC38E0 CRC64;
MEVLMLFSAL PAKQGLYDPE AEVDSCGVAM VTDIHGRRSH SIVSDGLLAL ENLEHRGAAG
AEANSGDGAG ILIQLPDELL RASVDFELPA PTASGVNTYA AGTCFLPRDP DLRSAAIARV
TDLAAAEGIT ILGWRELPVD ADGADIGETA LDCMPHMAQL FVTVDPGPGV TRIGGIDLDR
AIYPFRKQAE RVTPEIDAEG TGLYFPSLSS RTIVYKGMLT TMQLPLYYPD LRDERCMSAI
AIVHSRFSTN TFPSWPLAHP FRFVAHNGEI NTVRGNRNRM RAREALLETD LIPGDLKRAF
PICTPEASDS ASLDEVLELL HLGGRSVAHA VMLMVPEAWE NVPSMDPKRR AFLQFNGSLM
EAWDGPACVT FTDGAVVGAV LDRNGLRPGR WWQTRDGRVI LASEAGVLDV PVDDVVSKGR
LEPGKMFLVD TAAGRIIPDE EVKGDLINAE PYDEWLHAGL LDIATLPPRP VYTPNHDTVV
RRQVSFGYTE EDLRVLLTPM AASGYEPLGS MGTDTPVAVL SKRSRLLYDY FVELFAQVTN
PPLDAIREEI VTSMARVMGP EQNLLGPTAA SCRQILLHWP VIDNHDLAKL VHIDDDGDNP
GLSAKVLHGL YEVADGGPGL AAALEDLRLR ASQAIAEGHR TLVISDRHTD REHAPIPSLL
ATSAVHHHLV RTKERTKVAL VVESGDAREV HHIALLIGFG AAAVNPYLAL ESIEDLIAQG
ELIGVAASKA IRNYVEALGK GVLKVMSKMG ISTISSYTAS QAFEAVGLSS EVVREYFTRT
VSRIEGVGLD ELAEEVRMRH HRAFPENPTE QVYRRLEVGG EYQYRREGEL HVFTPETIFL
LQHATKTGRD DVFQKYSDEV DRLQREGGTL RGLFELDLGA RDPIPLEEVE PAEEIMKRFN
TGAMSYGSIS AEAHETIAIA MNRIGARSNS GEGGEDVDRL YDPERRSAVK QVASGRFGVT
SDYLINATDI QIKMAQGAKP GEGGQLPAYK VYPWIAKTRH STPGVALISP PPHHDIYSIE
DLAQLIHDLK NANSQARIHV KLVSAVGVGT VATGVSKAHA DVVLISGHDG GTGASPLTSL
KHAGTPWEIG LADAQQTLML NGLRDRITVQ CDGALRNGRD VIMAALLGAE EYGFSTAPLI
VTGCIMMRVC HLDTCPVGVA TQNPQLRARF SGQAEHIVNF FRFIAEDVRK YLAQLGYRTL
DEAVGQSQRL HTDAAVAHWK SKGLDLSPIF RRIEDKGPTR RVRGQDHGLD KALDQTLIQL
AEGALEDAHP VTLELPVRNV NRTVGTLLGA EVTRRYGAAG LAEDTITVEL TGSAGQSLGA
FLPPGVTIKL SGDTNDYVGK GLCGGKIVVA PHPDAWFIAE DQVIAGNTIL YGATSGQVYL
RGRVGERFSV RNSGATAVVE GVGDHACEYM TGGRVVILGP TGRNMAAGMS GGMAFVYDLD
PAKVNMAMVE LMRPDPDDLR WLHEHITIHT ELTGSAIGAS MLADWPRRCL AFTKVMPTDY
KRVLDAAQMA EAEGRDVDSA IMEAARG
//
