ID A0A0B4RFH2_9BACL Unreviewed; 1528 AA.
AC A0A0B4RFH2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glutamate synthase [NADPH] large subunit {ECO:0000313|EMBL:AIY06690.1};
GN ORFNames=Plano_2725 {ECO:0000313|EMBL:AIY06690.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY06690.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY06690.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY06690.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009129; AIY06690.1; -; Genomic_DNA.
DR RefSeq; WP_038705012.1; NZ_CP009129.1.
DR STRING; 1526927.Plano_2725; -.
DR KEGG; pln:Plano_2725; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_9; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000031496; Chromosome.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000031496}.
FT DOMAIN 22..420
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 908..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1528 AA; 168730 MW; 7281014AD52B2357 CRC64;
MSKKEYPIPQ GLYHPDQEHE ACGIGMIANI NGEKSHAIVQ NAINILCNLE HRGGQSSDTS
TGDGAGILTQ IPHRFFLKQC EKEGITLPEE GKYGIGMLFM PQDYDLRMKT KEMIHQIIQE
EGQICLGWRP VPVNDSFVGK VASKTKPVIR QVFIGAAHGL ENRIDLERRL YIIRKRIEQA
MLGKEDFKDV YFSSLSAGTI VYKGMLIPEQ LDSFYIDLNH PEFKSALALV HSRFSTNTFP
SWQRSHPNRY SIHNGEFNTL RGNVNWMRAR QVLCESPAFN KDDLKKVLPV IDETGSDSSM
FDNCFEFLHL SGRSLAHTAM MMVPEPWVND HTIKKEKRDF YEYHSTLMEP WDGPAALVFT
DGKQIAACLD RNGLRPARYY VTKSGMIVMG SEVGALDIFA DDIIYKDRLR PGKMLLVDLE
EGKIIPDEEI KLQIAGELPY KDFIDKNMFD MDDFPEPVMP SKSTNAEPLI KRQLAFGYTM
EEVQKIIKPL ATEGKDPVGS MGYDSPLAVL SKKPQLLYNY FKQLFAQVTN PPIDAIREHI
ITAARTTIGA EANLVQPTPE SARHIRLETP ILTNAELEKL RQQDLPVFKP ATISILFKKD
EGTAAMEKRL DAVFAEADQA IKDGAKLLIL SDRGVNEEYA AIPALLAVSG LHHYLIRQET
RIQMSILLES AEPREVHHFA ALLGYGAEGI NPYLAFDTIE NLIDIGDIPN VSFEEAETTY
VKAVTDGIIK VLSKMGISTI QSYRGAQIFE AVGIHMNVID KYFTRTSSRL GGIGLDIIAQ
EVLMRHATAY PVAQGDNQAL ESGDEFQYRE NGENHQYNPK TIHTLQHACR TNNYDVFKKY
TNLLTDEKAN LQSLRGLMSF KKRTPVPIDE VETVDEICAR FKTGAMSYGS ISKEAHEALA
VAMNRIGGRS NSGEGGEETS RFIPDENGDN RRSAIKQVAS GRFGVTSHYL VNADEIQIKV
AQGAKPGEGG HLPGKKVYPW IAEVRGSTPG VELISPPPHH DIYSIEDLAE LIFNLKNANP
SARISVKLVS AVGVGTIAAG VAKGRADVVL ISGYDGGTGA APKTSLKHTG LPWEIGLAET
HQTLLLNGLR DRIVVETDGK MMTGRDVVTA ALLGAEEFGF STAPLVVLGC VMMRVCHLDT
CPVGIATQNP ELREKYGGDP EHVVNFMRFI AREARELMAE LGFRTINEMI GRTDVIEANQ
AIDHWKAGGI DLTALLYQPD LPAKVGRYAT IKQNHELEQT LDYQELLPRC KKAIETGERV
EVATAIRNIH RATGTIVGSA ISKRYGAEGL PEDTVNLNFQ GSAGQSFGAF IPKGMTMNLI
GDANDFVGKG LSGGKILVYP ALDSTFIPEK NIIIGNVSFY GASAGEAYIY GVAGERFAVR
NSGANIVVEG VGDHGCEYMT GGRVAILGQT GKNFAAGMSG GIAYVLDEEG TFSERCNAEM
VHLQPLADPA EIEELREMIK KHVHYTSSRN GTRLLKNWDI YSAKFVRVIP KAYLQINERI
DKLQSGGMTR DEAEMAAFEE SKMAGAGK
//
