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Database: UniProt
Entry: A1T9W7_MYCVP
LinkDB: A1T9W7_MYCVP
Original site: A1T9W7_MYCVP 
ID   A1T9W7_MYCVP            Unreviewed;       525 AA.
AC   A1T9W7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ABM13967.1};
GN   OrderedLocusNames=Mvan_3165 {ECO:0000313|EMBL:ABM13967.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM13967.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM13967.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
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   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000511; ABM13967.1; -; Genomic_DNA.
DR   RefSeq; WP_011780372.1; NC_008726.1.
DR   AlphaFoldDB; A1T9W7; -.
DR   STRING; 350058.Mvan_3165; -.
DR   KEGG; mva:Mvan_3165; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_011398_4_4_11; -.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
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.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT   DOMAIN          21..462
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   525 AA;  54934 MW;  2A109BB97F6D741A CRC64;
     MQHIPETVNV GDVTSWSDEV DVVVVGFGIA GGCAAVSAAA AGARVLVLEK AAAVGGTTSM
     AGGHFYLGGG TAVQQATGHD DSAEEMYKYL VSQSRDPEHD KIRAYCEGSV EHFNWLEALG
     FQFERSYYPG KVVVPPGTEG LSYTGNEKVW PFCEQAKPAP RGHSVPVPGE LGGAAMVIDL
     LLKRAADLGV QIRYETGVTG LVVDDDGAVV GVRWKHFTET GEVKAKSVVI AAGGFAMNAE
     MVAEYTPALA AERKTKHHGT VAPYILGNPN DDGLGIKLGV SAGGVAANLD QLFITAAAYP
     PEILLTGVIV NKDGQRFVAE DSYHSRTSAF VLEQPEQTAY LIVDEDHMQM PEMPLIKFVD
     GFETIAEIES ALGIPDGNLA ATLECYNANA AAGVDPDFHK QPEYLAAQDK GPWAVFDLSL
     GRAMYSGFTM GGLTVSIDGE VLREDGSAIP GLYAAGACAC NIAQDGKGYA SGTQLGEGSF
     FGRRAGEAAA RRAGEAAARR AGEAAARRAG EAAARRAGEA AAERA
//
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