ID A0A2N3PVW3_9PROT Unreviewed; 434 AA.
AC A0A2N3PVW3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
GN ORFNames=CWS72_10640 {ECO:0000313|EMBL:PKU24549.1};
OS Telmatospirillum siberiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Telmatospirillum.
OX NCBI_TaxID=382514 {ECO:0000313|EMBL:PKU24549.1, ECO:0000313|Proteomes:UP000233293};
RN [1] {ECO:0000313|Proteomes:UP000233293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26-4b1 {ECO:0000313|Proteomes:UP000233293};
RA Hausmann B., Pjevac P., Schreck K., Herbold C.W., Daims H., Wagner M.,
RA Pester M., Loy A.;
RT "Draft genome sequence of Telmatospirillum siberiense 26-4b1T, an
RT acidotolerant peatland alphaproteobacterium potentially involved in sulfur
RT cycling.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Could be required for the formation of a functional
CC nitrogenase Fe protein. Probably accepts electrons from FixA/FixB and
CC reduces a quinone. {ECO:0000256|ARBA:ARBA00003676}.
CC -!- FUNCTION: Part of an electron transfer system.
CC {ECO:0000256|RuleBase:RU366069}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU366069};
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family.
CC {ECO:0000256|ARBA:ARBA00006796, ECO:0000256|RuleBase:RU366069}.
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:PKU24549.1}.
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DR EMBL; PIUM01000010; PKU24549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3PVW3; -.
DR OrthoDB; 417034at2; -.
DR Proteomes; UP000233293; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039651; FixC-like.
DR PANTHER; PTHR43624; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR PANTHER; PTHR43624:SF2; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU366069};
KW Flavoprotein {ECO:0000256|RuleBase:RU366069};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366069};
KW Reference proteome {ECO:0000313|Proteomes:UP000233293}.
SQ SEQUENCE 434 AA; 47941 MW; 6835314B02BF058C CRC64;
MSQEKFDAIV VGAGPSGNAA AYTLARKGLN VLQLERGEYP GSKNVQGAIL YAKALEEIIP
DFRESAPLER HIIEQRLWML DDSSYVGMHY RSEDFNEDRP SRYTILRAQF DKWFSQQVRD
AGAVLLCETT VTELLRDESG RVIGVATDRD NGTVYADVVI LAEGVNGLVG RRSKLREELQ
PESVALAVKE MHFLPKDVID ARFNLKGGEG VVIEGMGTIT EGMTGTAFIY TNNESLSVGI
GCLVSDLAQT GRSPAGLLEA FKNHPSVKPL LAGSEIKEYA AHLIPEGGLK AMPELFGDGW
IVVGDAGHFV NAVHREGSNL AMTTGRLAAE TVADLKQRGV PCSKANLRAY TKRLEDCFVM
KDMKKYKDIP SFLHGNRHLF DLYPRLVSKA AQNWFRVDGK DKLTKEKEIL TSFRKGRTLS
GLLGDAFKMA RAWR
//
