ID H3KDD3_9BURK Unreviewed; 506 AA.
AC H3KDD3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Flavocytochrome c {ECO:0000313|EMBL:EHY31869.1};
GN ORFNames=HMPREF9440_00742 {ECO:0000313|EMBL:EHY31869.1};
OS Sutterella parvirubra YIT 11816.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY31869.1, ECO:0000313|Proteomes:UP000004956};
RN [1] {ECO:0000313|EMBL:EHY31869.1, ECO:0000313|Proteomes:UP000004956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY31869.1,
RC ECO:0000313|Proteomes:UP000004956};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|RuleBase:RU366062}.
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:EHY31869.1}.
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DR EMBL; AFBQ01000103; EHY31869.1; -; Genomic_DNA.
DR RefSeq; WP_008541410.1; NZ_JH604916.1.
DR AlphaFoldDB; H3KDD3; -.
DR STRING; 762967.HMPREF9440_00742; -.
DR PATRIC; fig|762967.3.peg.594; -.
DR HOGENOM; CLU_011398_4_5_4; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000004956; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU366062};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366062};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366062};
KW Reference proteome {ECO:0000313|Proteomes:UP000004956}.
FT DOMAIN 43..483
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 506 AA; 54182 MW; A9A03FED7F65A632 CRC64;
MSNIETSRRR FLIGAAAGAA VMAGEAVAAK PAADTPKFDK VYDIIVVGSG FAGLAAALEA
RLGGAEVLLI EKMPAFGGNS AINGGAFSVA GTPLQKKAGI KDSPKQMLAD MIKSGRGLSH
VPLLKMVVDG SLPAYEFTLR HGVKYKDFVQ HFGGHSVPRT LQTVESTGGG ITRPLTESCK
QHGVDMHLRA KMEKFVRDES GRVIGLEVRE GYLFPKETSG VMQTYGVRKG VIMATGGFSR
NLWFRMQQDP NLDERLDSTN HLGATGEGLL SMLAIGGAPV QIDQIQLGPW CSPDERGFGL
VSQFNTIAGF PMGIMVDVRN GRRFCNELAD RKERTDAILG LMENGKPVYP VCFTDSKGVE
KAQTLKNGLK YGVIKQFDKV EDLAKAYGIP ADALVKQVAE WNEMVEKKDD TAFHRALDLA
IKLDKPPFYA CRVWPKVHYC MGGVGITAKA EVVDVMGKVM PGLYACGEVT GGTHGASRLG
GCAIADGLVM GRVAADSALK AEAVKL
//
