ID A0A0N0N434_9ACTN Unreviewed; 541 AA.
AC A0A0N0N434;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamate synthase (NADPH), 3-methyl-2-oxobutanoate dehydrogenase (Ferredoxin) {ECO:0000313|EMBL:KPI19031.1};
DE EC=1.2.7.7 {ECO:0000313|EMBL:KPI19031.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KPI19031.1};
GN ORFNames=OK074_1495 {ECO:0000313|EMBL:KPI19031.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI19031.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI19031.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI19031.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI19031.1}.
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DR EMBL; LJCV01000055; KPI19031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N434; -.
DR PATRIC; fig|1592327.3.peg.1709; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43100:SF2; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE, CHLOROPLASTIC-LIKE; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KPI19031.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 480..510
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 511..540
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 541 AA; 58551 MW; B2DCCBD0A68D00D6 CRC64;
MKEKPFAITL DVGSSLANHT GAWRTERPEY VDRLPPCNQA CPAGENIQQW LFHAESGDYE
SAWRQLMRDN PLPAVMGRVC YHPCETACNR VQVDNAVGIN SVERFLGDEA IKRGWSVEAP
PVTSGKRVLV VGSGPAGLSV AYQLRLLGHE VTIREAQEQP GGMMRYGIPR YRLPREVLDA
EIDRIVALGV TLELNTRVDD VLAAQRDEGF DAVFLAVGAG IGRRAYIPAG DSARILDAVA
LLGGMEGADR PLLGRRVAVY GGGNTAMDAA RTARRLGATD AVVVYRRTRD RMPAHDVEVE
EALEEGVRMK WLSTIKHAEE GHLTIERMAL DETGFPQPTG EFEELQADTV VLALGQESDL
SLLKSVPGLS VDHGTVQVAD GLMTGHRGIF AGGDMVPADR TVTVAVGHGK KAARHIDAYL
RGSSYDPGAK HDPAAFENLN TWYYADAPAS VRPRLELARR VSTFDEVVHG LDESTALFEA
RRCMSCGNCF ECDNCYGVCP DNAITKLGPG KGFSIDLDYC KGCGLCAAEC PSGAIGMVPE
E
//
