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Database: UniProt
Entry: W1SND7_9BACI
LinkDB: W1SND7_9BACI
Original site: W1SND7_9BACI 
ID   W1SND7_9BACI            Unreviewed;       337 AA.
AC   W1SND7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Pyruvate/ketoisovalerate oxidoreductase subunit gamma {ECO:0000313|EMBL:ETI69514.1};
GN   ORFNames=BAVI_07009 {ECO:0000313|EMBL:ETI69514.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI69514.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI69514.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI69514.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
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:ETI69514.1}.
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DR   EMBL; ALAN01000050; ETI69514.1; -; Genomic_DNA.
DR   RefSeq; WP_024027613.1; NZ_ALAN01000050.1.
DR   AlphaFoldDB; W1SND7; -.
DR   STRING; 220686.AA980_01655; -.
DR   PATRIC; fig|1131730.3.peg.1451; -.
DR   eggNOG; COG1014; Bacteria.
DR   eggNOG; COG1144; Bacteria.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000018877; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR   Gene3D; 3.30.70.3270; -; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011894; PorC_KorC.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   NCBIfam; TIGR02175; PorC_KorC; 1.
DR   PANTHER; PTHR43366; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR   PANTHER; PTHR43366:SF1; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR   Pfam; PF13237; Fer4_10; 1.
DR   Pfam; PF01558; POR; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:ETI69514.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT   DOMAIN          247..276
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          285..316
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   337 AA;  37562 MW;  C310EBCC09CDD54E CRC64;
     MSILPKKNEL GFFEIRLESI GGLGANLAGK MLAEAGVFSL GLKGSNFSSY GSEKKGSPVK
     SFVRFCDPDV EIRDHSPIEQ PHIVGVFHEA LYKTVNVVSG LNADGIVLVN TARDFDDVRH
     DLQLEYGTLA IVDALTIAVE EKTKVNTAML GALYRICDFL DPESMRDVIR KTFTKKYPHL
     VEPNIRTFDR GYNEVQFKTY DVPESAEGKK FTRALPQLGY MTQEIGGVIV SQANSIFKDL
     GGSRQGFLPE FQQDKCIHCA ACDNVCPDFC FVWEDGEDKR GRKQMFLQGI DYQFCKGCLK
     CVEACPTDAL GNLRELIGYA DEHRVKQNFP YVSGGSY
//
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