ID   N6X608_9RHOO            Unreviewed;       487 AA.
AC   N6X608;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:ENO77176.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:ENO77176.1};
GN   Name=gltD {ECO:0000313|EMBL:ENO77176.1};
GN   ORFNames=B447_16267 {ECO:0000313|EMBL:ENO77176.1};
OS   Thauera sp. 27.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO77176.1, ECO:0000313|Proteomes:UP000013140};
RN   [1] {ECO:0000313|EMBL:ENO77176.1, ECO:0000313|Proteomes:UP000013140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=27 {ECO:0000313|EMBL:ENO77176.1,
RC   ECO:0000313|Proteomes:UP000013140};
RA   Liu B., Shapleigh J.P., Frostegard A.H.;
RT   "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:ENO77176.1}.
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; AMXB01000033; ENO77176.1; -; Genomic_DNA.
DR   RefSeq; WP_002925803.1; NZ_AMXB01000033.1.
DR   AlphaFoldDB; N6X608; -.
DR   eggNOG; COG0493; Bacteria.
DR   Proteomes; UP000013140; Unassembled WGS sequence.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; 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; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ENO77176.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013140}.
FT   DOMAIN          37..68
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   487 AA;  53081 MW;  AF98533982F76B15 CRC64;
     MGKPTGFLEH QRLSEAYEPV DKRLKTYKEF VLRLTDEQAS VQGARCMDCG IPFCNNGCPV
     NNIIPDWNDL VYRGHWREAI EVLHSTNNFP EFTGRICPAP CEAACTLNIN TDAVGIKSIE
     HAIIDKAWEE GWVLPLPPET RTGKKVAVVG SGPAGLAAAQ QLARAGHDVT VFEKNDRIGG
     LLRYGIPDFK MEKGLIDRRV EQMQAEGVRF RTGVLVAAKD MPAGIVNDAK EVISAEQLQK
     DFDAVVLAGG AEVPRDLPVP GRELGGVHYA LEFLIPQNKQ VAGDKPNPIS AKGKHVVVIG
     GGDTGSDCVG TSNRHGAASV TQFELMPMPP EQENKPLVWP YWPTKLRTSS SHEEGCERDF
     AVATKEFIGK NGKVKALKAC RLEWKDGRMS EVPGSEFEIK ADLVLFAMGF TQPVGGVLEA
     FGVDKDARGN AKATTDGEGC YTTNVPKVFA AGDMRRGQSL VVWAIREGRQ CARAVDEFLM
     GESLLPR
//