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Database: UniProt
Entry: A4Y870_SHEPC
LinkDB: A4Y870_SHEPC
Original site: A4Y870_SHEPC 
ID   A4Y870_SHEPC            Unreviewed;       517 AA.
AC   A4Y870;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=Flavocytochrome c {ECO:0000313|EMBL:ABP76153.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sputcn32_2432 {ECO:0000313|EMBL:ABP76153.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP76153.1};
RN   [1] {ECO:0000313|EMBL:ABP76153.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 {ECO:0000313|EMBL:ABP76153.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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}.
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DR   EMBL; CP000681; ABP76153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4Y870; -.
DR   STRING; 319224.Sputcn32_2432; -.
DR   KEGG; spc:Sputcn32_2432; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_011398_4_5_6; -.
DR   OMA; QPGQIAY; -.
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   PRINTS; PR00368; FADPNR.
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}.
FT   DOMAIN          49..491
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   517 AA;  55309 MW;  79023640905B5781 CRC64;
     MSKTQDIDTG RRQLLKGGAV MAAGFGAAIA LPATANCGVA PEVFDEIVDV LVVGSGFAGM
     SAALQAREAG VSVMVVDKMP VFGGNSTING GAMAVAGSEL QKQAGIKDSV DEMVADMMRA
     GRGMNDVEML KLVCNGTAES CQWLIEHGVK WKPFVQHFGG HSIQRVLQTV ESSGAGIIRP
     LINAARDKGV VMRNQTKLES FVKDLDGRVI GVEVREGFYF PNERTGKIRR IGARRGVVMA
     TGGFGRDIEY RMMQLPELNN DLDSTNHAGA TSEALKQMML LGANPIHLDQ IQLGPWASPD
     EKGFGTASQF NTIATYPHGI VVDVRTGERF FNELADRKAR ADAIMTRRDE HGQPVYPIGF
     TNAEGASKAQ TLDWGLKYKV ISKAETLDEL AAIYGMPAKA LKAQVARWNE AVKSGVDKEF
     ARPLQEAIVL DKGPWYAVRM WPKVHYCMGG VKVNTRSEVL HLVTNQAIPG LYAAGEATGG
     IHGASRLGAC AVAEGVVTGR NAGRNCAAAK AAVLKQA
//
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