ID E2SGV3_9FIRM Unreviewed; 467 AA.
AC E2SGV3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Rubredoxin {ECO:0000313|EMBL:EFP63210.1};
GN ORFNames=HMPREF0983_00192 {ECO:0000313|EMBL:EFP63210.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP63210.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP63210.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP63210.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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:EFP63210.1}.
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; ACTJ01000004; EFP63210.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SGV3; -.
DR STRING; 658659.HMPREF0983_00192; -.
DR eggNOG; COG0069; Bacteria.
DR HOGENOM; CLU_023342_0_1_9; -.
DR BioCyc; EBAC658659-HMP:GMFE-198-MONOMER; -.
DR Proteomes; UP000006223; Unassembled WGS sequence.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR CDD; cd02808; GltS_FMN; 1.
DR CDD; cd00730; rubredoxin; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024188; GltB.
DR InterPro; IPR043578; GltB_archl_type.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
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 Pfam; PF00301; Rubredoxin; 1.
DR PIRSF; PIRSF500061; GOGAT_lg2_archl; 1.
DR PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..43
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 467 AA; 51175 MW; 1FF0F67247DA57AD CRC64;
MKYVCEICGY IYDETAEGTP WNNLDDTWSC PLCTAPKACF KPDKTEESDK QITNTNKNTS
TLSIQKNAKK EDILESNLSL IHEMSVHGSS RIEAMRTRKP VPGWDDILLL GGQLSNPPLA
DKADVDTTTI IGKHARKPMV LEHAVYVSHM SFGALSKEAK TALSMGTAAV HTAQCSGEGG
ILPDEINHAY KYIFEYVPNK YSVTDENLKR SDAIEIKIGQ GSKPGMGGHL PAEKVTEEIS
AIRGKPLHKD IISPSKFEEI KTKDDLKNLV SSLRERSEGR PIGIKIAAGH IEADLEWIAY
AQPDFITIDG RGGATGASPK YLKDNATVPT VYALARARAY MDKHHMSQEL IITGGFRTSG
EMIKALAMGA DAVAIASAAM MAIGCQQYRI CHNGKCPMGI ATQDPELRKN FSIEKGAKRL
ENYLNVLREE LKSFARISGH TSIHDLSEDD LCTTSSEISN HTNIPHC
//
