ID G2FKP6_9FIRM Unreviewed; 435 AA.
AC G2FKP6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=FMN-dependent dehydrogenase family protein {ECO:0000313|EMBL:EGW41772.1};
GN ORFNames=DOT_0249 {ECO:0000313|EMBL:EGW41772.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW41772.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW41772.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW41772.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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:EGW41772.1}.
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DR EMBL; AGAF01000013; EGW41772.1; -; Genomic_DNA.
DR RefSeq; WP_009612963.1; NZ_AGAF01000013.1.
DR AlphaFoldDB; G2FKP6; -.
DR PATRIC; fig|913865.3.peg.232; -.
DR eggNOG; COG0069; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000004928; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR024188; GltB.
DR InterPro; IPR043578; GltB_archl_type.
DR InterPro; IPR002932; Glu_synthdom.
DR PANTHER; PTHR43819:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR PIRSF; PIRSF500061; GOGAT_lg2_archl; 1.
DR PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}.
FT DOMAIN 321..409
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 435 AA; 46740 MW; 9D7CC46509A55932 CRC64;
MNEETKVKEP TDSVKSLWHK DTLAEIDYKA RAGKHRIRGC ATPRRMPNFD DLMILPGQLT
RMTIDTYRED CETRTVLGKR FAKKPLVIET PVMIGGMSYG ALSKEAKTAL AKATSLVGTV
ISNGEGGILP EELENSYRQS IQVLASRMGF TKRNLEVADM LEFVYGIGAK PGLSGHLMGS
KISAEVAELR KLPIGIDLHS HPRSGDSFGA DDMIIKMEQM RELTNWEVPI FVKMAAGRVR
EDIKIAVKLG IDGIILDGCQ AGTGAAPVMA ADHLGIPTMP ALVQAVRTLE EMGVKDEVSL
IISGGIRDGA DLAKALAIGA DAVAIGTSAL IAMGCRVCMR CHTGNCSFGI GTQNPEQRKN
LDIDEAAERV ANYIQAMTAE AVLLAKAAGK SKLKNMERED LRALTLETAA MTGIPLVGSD
LVIGEGFGFT ANNKI
//
