ID W8RZZ5_9RHOB Unreviewed; 1514 AA.
AC W8RZZ5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glutamate synthase [NADPH] large chain {ECO:0000313|EMBL:AHM03417.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AHM03417.1};
GN ORFNames=roselon_01017 {ECO:0000313|EMBL:AHM03417.1};
OS Roseibacterium elongatum DSM 19469.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseibacterium.
OX NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM03417.1, ECO:0000313|Proteomes:UP000019593};
RN [1] {ECO:0000313|EMBL:AHM03417.1, ECO:0000313|Proteomes:UP000019593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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; CP004372; AHM03417.1; -; Genomic_DNA.
DR RefSeq; WP_025311289.1; NZ_CP004372.1.
DR STRING; 1294273.roselon_01017; -.
DR KEGG; red:roselon_01017; -.
DR PATRIC; fig|1294273.3.peg.997; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_5; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000019593; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) 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:AHM03417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019593}.
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 912..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1514 AA; 164764 MW; 693047B585D9B4D4 CRC64;
MTKYDADWAA AEQAKREWMA ENAMFREEDE HSSCGVGLVV SIDGKPSRAV VENGISALKA
IWHRGAVDAD GKTGDGAGIH VQIPVHFFYD QVRRTGHEPR MNELMAVGQV FLPRNDFGAQ
ETCRTIVESE VLRMGYYIYG WRHVPVDITV LGEKANATRP EIEQIIISNS KGVDEETFER
ELYVIRRRIE KAAAAAQVGQ LYLCSLSCRS IIYKGMMLAQ DVAEFYPDLK DERFESAFAI
YHQRYSTNTF PQWWLAQPFR MLAHNGEINT LKGNVNWMKS HEIRLSSAYF GEMAEDIKPI
IAQGASDSAA LDAVFEVLVR AGRSAPMAKT MLIPEAWSQT ASKLPQAWQD MYSYCNSVME
PWDGPAALAM TDGRWVCAGL DRNGLRPMRY VVTGEGLLIA GSEAGMVPVD EATVVEKGAL
GPGQLIAVDM AEQKLFHDTE IKDALAASRP FGDWVGKITD LAIETNGVTE TAIFEATELR
KRQVAAGYSM EELEQILAPM AEDGKEAIAS MGDDTPAAVL SSMYRPLSHY FRQNFSQVTN
PPIDSLREYR VMSLKTRFGN LKNVLDEDSS QTEILVLDSP FVGNAQFDEM VKHFGASLVT
IDCTFPVGGK SGALRDNLAR IRQEAEDAVR SGAGHIVLTD RFQSEDRVPM PMILATSAVH
SWLTRQGLRT FCSLNVRSAE CIDPHYFAVL VGCGATTVNA YLAQDSIADR IERGLIDGTL
TEAMARYRAS IDAGLLKIMS KMGISVISSY RGGLNFEAVG LSRAMVNEYF PGMLSRISGI
GVSGLQKKVE EVHAKGWQGG ADVLPLPIGG FYKARRSGEK HAWEAQTMHM MQMACNRSSY
ELWKQYSKKM QSNPPIHLRD LLDMKPLGEP INIEEVESIT SIRKRFVTPG MSLGALSPEA
HKTLNVAMNR IGAKSDSGEG GEDPAHFVPE PNGDNPSAKI KQVASGRFGV TAEYLNHCEE
LEIKVAQGAK PGEGGQLPGM KVTDLIARLR HSTKGVTLIS PPPHHDIYSI EDLAQLIYDL
KQINPRCKVT VKLVASSGVG TIAAGVAKAK ADVILISGHN GGTGASPATS IKYAGLPWEM
GLTEAHQVLA MNKLRDRVTL RTDGGLRTGR DIVMAAMMGA EEYGIGTAAL IAMGCIMVRQ
CQSNTCPVGV CTQDPALREK FTGNADKVVN LITFYAQEVR EILASIGARS LDDVIGRADL
LTQVSRGAAH LDDLDLNPML ITVDGADRIV YDRYKPRNAV PDTLDAQIVK DAHRFLEDGE
KMQLSYAVQN TLRTIGTRTS SHIVKNFGMR NHLQPDHLTV KLEGSAGQSL GAFAAPGLKL
EVSGDANDYV GKGLSGGTIV VKPPQVSPLK ADDNVIVGNT VLYGATDGYL FAAGRAGERF
AVRNSGAKVV VEGCGSNGCE YMTGGVAVIL GSIGANFGAG MTGGMAYLHD PEGQTGVNMN
METLVTCPVT VDHWEQQLRG LIERHAKETG SRKAADILQH WDLERGNFVQ VVPKEMLDKL
AHPVGIEAGA VPAE
//
