ID A0A0S8B675_9CHLR Unreviewed; 496 AA.
AC A0A0S8B675;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KPK07125.1};
GN ORFNames=AMJ56_13735 {ECO:0000313|EMBL:KPK07125.1};
OS Anaerolineae bacterium SG8_19.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK07125.1, ECO:0000313|Proteomes:UP000050892};
RN [1] {ECO:0000313|EMBL:KPK07125.1, ECO:0000313|Proteomes:UP000050892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_19 {ECO:0000313|EMBL:KPK07125.1};
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 -!- 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:KPK07125.1}.
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DR EMBL; LJNN01000182; KPK07125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8B675; -.
DR PATRIC; fig|1703386.3.peg.286; -.
DR Proteomes; UP000050892; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; 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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 29..140
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 153..478
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 496 AA; 54824 MW; DBBF13B4248C8438 CRC64;
MGKATGFMQY SRETPDSRPI IERLGDWHSF HVPMVESRLQ QQAARCMDCG IPFCHTGSIL
NGMTTGCPLH NLIPEWNDLV YRGLWREAYE RLAKTNNFPE FTGLVCPAPC EAGCTLGIYD
PPVTIKSIEY AIVEKAFHEG WVKPELPRRR TGKKVAVVGS GPAGLACADQ LNRVGHQVTV
FERADRVGGL LTYGIPNMKL EKGTVERRIG LMVAAGVKFL TSTEVGIHYP AEKLGQEFDA
IVLCLGAARP RDLPVAGRGL KGIHYAVDYL HANTKSLLDS GHQDNQFISA RDKDVIVIGG
GDTGTDCVAT ALRHGCRSLV QLEIMPRPPE IRGPDNPWPQ WPQIYKLDYG QEEAEAVFGR
DPRRYSVMTK AFLGDENGQV KALQTIDVRW EKSLNGSSRP VLQELPGNER NWPAQLVLLA
MGFLGPEKNL LEQLAIERDD RSNARADYGR FSTSEPGIFA AGDVRRGQSL VVWAINEGRG
AARECDRYLM GTTSLP
//