ID A0A0U2XJN8_9MICC Unreviewed; 661 AA.
AC A0A0U2XJN8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:ALU38578.1, ECO:0000313|EMBL:GEO93213.1};
DE EC=1.3.5.1 {ECO:0000313|EMBL:ALU38578.1};
GN Name=sdhA {ECO:0000313|EMBL:ALU38578.1};
GN Synonyms=sdhA_2 {ECO:0000313|EMBL:GEO93213.1};
GN ORFNames=AS188_01100 {ECO:0000313|EMBL:ALU38578.1}, KFL01_25190
GN {ECO:0000313|EMBL:GEO93213.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU38578.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU38578.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU38578.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO93213.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO93213.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013254; ALU38578.1; -; Genomic_DNA.
DR EMBL; BJZR01000094; GEO93213.1; -; Genomic_DNA.
DR RefSeq; WP_058857292.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U2XJN8; -.
DR STRING; 446860.AS188_01100; -.
DR KEGG; kfv:AS188_01100; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; Unassembled WGS sequence.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal 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 ECO:0000313|EMBL:ALU38578.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000057181}.
FT DOMAIN 54..459
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 521..660
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 661 AA; 72493 MW; E2DE23B2DCB5D00B CRC64;
MSVRTTTQSS PAQSTTEGQV LDGRAPGGDP ATAWGRRKLE YRLVSPLNRR KFTVIVVGTG
LAGAGCAAAL GELGYHVVAY TIHDSARRAH SVAAQGGINA ARARKVDNDS LERFVKDTIK
GGDFRAREAD CFRLAEESVR VIDHATAIGA PFAREYGGQL RTRSFGGVQV SRTFYTRGQT
GQQLEVAAFR SLQRQVAAGT VELRTRQEML DVIVTDGRAQ GVVTRDLHTG QIEAQTAHAV
VLATGGYGSV FHKSTLARNS NVTAAWRAHR RGAYFASPSF IQFHPTALPV SSRWQSKTTL
MSESLRNDGR IWVPARPGDD RSPGEIPEQE RDYYLERKYP AYGNLAPRDI SSRAAREQIA
AGHGVGPLRN SVYLDFQDAI DRWGMQVIKE RYGNLFEMYF DATGEDPFTV PMRIAPGAHF
AMGGLWSDYN MMTSIPGLFV AGEAGWGYHG ANRLGANSLL SACVDGWFTL PYAVPDYLAG
QLGQPVLSVQ DPAVQATISA VQQRTDRLLS IGGTQGADRF HARLGEILYT GCGVSRSAAG
LTEALEQIRG LREQFWADLR VPGRGHQLNQ ELERAGRVAD FLDMGELMCL DALDREESCG
AHFREEHQTP EGEALRDDAN WCFVSAWEHT PGTDKVHPGL PVRHTEPLDF TVVQLQTRNY
T
//