ID A0A0S8BGI8_9PROT Unreviewed; 468 AA.
AC A0A0S8BGI8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KPK10712.1};
GN ORFNames=AMJ68_08280 {ECO:0000313|EMBL:KPK10712.1};
OS Acidithiobacillales bacterium SG8_45.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703383 {ECO:0000313|EMBL:KPK10712.1, ECO:0000313|Proteomes:UP000053136};
RN [1] {ECO:0000313|EMBL:KPK10712.1, ECO:0000313|Proteomes:UP000053136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_45 {ECO:0000313|EMBL:KPK10712.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK10712.1}.
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DR EMBL; LJTU01000039; KPK10712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BGI8; -.
DR PATRIC; fig|1703383.3.peg.1058; -.
DR Proteomes; UP000053136; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR006006; GltD-like.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01318; gltD_gamma_fam; 1.
DR PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR42783:SF3; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 23..133
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 146..455
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 468 AA; 51568 MW; F53F685F61DA4A06 CRC64;
MGNNFQFIQI ERHDPEKKPA EVRVKEYREI YGAFNSARAA EQADRCLHCG NPYCEWKCPV
HNYIPNWLKL VTEGNLGEAA ELSHRTNSLP EITGRVCPQD RLCEGACTLN DGFGAVTIGS
IEKYISDSAF DQGWRPDLSQ VHDTGKKVAV IGAGPAGLSC ADVLARNGVK AVVFDRYPEI
GGLLTFGIPE FKLEKEVVKR RRDIFEEMGI EFRLNTEVGK DISFDELLGE YDAVFLGMGT
YTYMKAGIPG EDLAGVYPAL DYLISNVNHC HGYEKDPADY LSMQGKRVVV LGGGDTAMDC
NRTSIRQGAE SVVCAYRRDE ANMPGSKREV ANAKEEGVQF KFNRQPIEIV GNGKVEGIKV
VTTELGEPDE RGRRRPEPVP GSEEIIPADS VIVAFGFQPS PADWFAGAKI EIDERGRVKA
PAGQEHKHQT TNPKIFAGGD MVRGSDLVVT AIWEGREAAE GMLDYLEV
//
