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Database: UniProt
Entry: S5STY3_RHIET
LinkDB: S5STY3_RHIET
Original site: S5STY3_RHIET 
ID   S5STY3_RHIET            Unreviewed;       369 AA.
AC   S5STY3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Electron transfer flavoprotein nitrogen fixation protein FixB {ECO:0000313|EMBL:AGS25417.1};
GN   Name=fixB {ECO:0000313|EMBL:AGS25417.1};
GN   ORFNames=REMIM1_PE00330 {ECO:0000313|EMBL:AGS25417.1};
OS   Rhizobium etli bv. mimosae str. Mim1.
OG   Plasmid pRetMIM1e {ECO:0000313|EMBL:AGS25417.1,
OG   ECO:0000313|Proteomes:UP000015261}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1328306 {ECO:0000313|EMBL:AGS25417.1, ECO:0000313|Proteomes:UP000015261};
RN   [1] {ECO:0000313|EMBL:AGS25417.1, ECO:0000313|Proteomes:UP000015261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mim1 {ECO:0000313|EMBL:AGS25417.1,
RC   ECO:0000313|Proteomes:UP000015261};
RC   PLASMID=Plasmid pRetMIM1e {ECO:0000313|Proteomes:UP000015261};
RA   Rogel M.A., Bustos P., Santamaria R.I., Gonzalez V., Romero D.,
RA   Cevallos M.A., Lozano L., Ormeno-Orrillo E., Martinez-Romero E.;
RT   "Genomic basis of Rhizobium etli symbiovar mimosae and its prevalence among
RT   Phaseolus vulgaris nodule bacteria.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in a redox process involved in nitrogen
CC       fixation. {ECO:0000256|ARBA:ARBA00003554}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000089-1};
CC       Note=Binds 1 FAD per dimer. {ECO:0000256|PIRSR:PIRSR000089-1};
CC   -!- SUBUNIT: FixA and FixB form a heterodimer.
CC       {ECO:0000256|ARBA:ARBA00011874}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000256|ARBA:ARBA00005817}.
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DR   EMBL; CP005955; AGS25417.1; -; Genomic_DNA.
DR   RefSeq; WP_020923574.1; NC_021909.1.
DR   AlphaFoldDB; S5STY3; -.
DR   KEGG; rel:REMIM1_PE00330; -.
DR   PATRIC; fig|1328306.3.peg.5839; -.
DR   HOGENOM; CLU_034178_1_1_5; -.
DR   Proteomes; UP000015261; Plasmid pRetMIM1e.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   CDD; cd01715; ETF_alpha; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR001308; ETF_a/FixB.
DR   InterPro; IPR033947; ETF_alpha_N.
DR   InterPro; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR   PANTHER; PTHR43153:SF1; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000089-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Plasmid {ECO:0000313|EMBL:AGS25417.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          32..223
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         273..274
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         287..291
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         304..311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         325
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   369 AA;  39581 MW;  936D6C14B8CD2BA7 CRC64;
     MLSTNRESPP PAVGRAAMKK ELPEKFKAHR HVWVFIELER GQVHPVSFEL LGEGRKLADK
     LGVQLAGVVL GPPGEFTWFA IAEAFAYGAD LAYLVEAPLL ADYRNEPFTK ALTELVTTYK
     PEILLLGATT LGRDLAGSVA TTLLTGLTAD CTELDVDADG SLAATRPTFG GSLLCTIYTL
     NCRPQMATVR PRVMAMPQRG NNQIGRVIQH DVPMIEEEIV TKVLGFLSDG LSATANLAYA
     DVVVAGGLGL GAAENLNLVK KLAQTIGADY GCSRPLVQKG WMPADRQIGQ TGKTIRPKLY
     IAAGISGAIQ HRVGVEGADL ILAINTDPNA PIFDFAHLGV VTDAIRLLPS LTELFTHRLS
     PHSRDKLAN
//
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