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Database: UniProt
Entry: H6N1V6_GORPV
LinkDB: H6N1V6_GORPV
Original site: H6N1V6_GORPV 
ID   H6N1V6_GORPV            Unreviewed;       658 AA.
AC   H6N1V6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Succinate dehydrogenase, flavoprotein subunit SdhA {ECO:0000313|EMBL:AFA74626.1};
GN   Name=sdhA2 {ECO:0000313|EMBL:AFA74626.1};
GN   OrderedLocusNames=GPOL_c36140 {ECO:0000313|EMBL:AFA74626.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA74626.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA74626.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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DR   EMBL; CP003119; AFA74626.1; -; Genomic_DNA.
DR   RefSeq; WP_014360989.1; NC_016906.1.
DR   AlphaFoldDB; H6N1V6; -.
DR   STRING; 1112204.GPOL_c36140; -.
DR   KEGG; gpo:GPOL_c36140; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_7_0_11; -.
DR   OMA; RFDEYFV; -.
DR   Proteomes; UP000009154; Chromosome.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProt.
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   Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT   DOMAIN          57..462
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          524..657
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        351
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   658 AA;  71656 MW;  95DC28E82066E139 CRC64;
     MNADAAATTG SDDPASRRLD SDALESSVPE GDPATAWRRR RDSYRLVGPL NRRKFTVIVV
     GTGLAGAGCA AALGELGYQV KSFTFHDAPR RAHSVAAQGG INAARARKVD NDSIHRFVVD
     TVKGGDFRGR EADAFRLAEE SIRVIDHLNA IGAPFAREYG GALSTRSFGG VQVSRTYYTR
     GQTGQQLQVA ASQALLRQVA AGSVTLHTRQ EMLDLVVADG RAQGIITRDL VTGEIAAQTA
     HAVVLATGGY GTVYFQSTLA RNCNATASWR AHRRGALLAS PSFIQFHPTA LPVSAPWQTK
     TTLMSESLRN DGRIWVPRKA GDDRPPGDIP DAERDYYLER KYPTYGNLTP RDVASRAARE
     QIESGHGVGP LHNSVYLDFA DALARLGRPT IAERYGNLFT MYRDATGEDP YEVPMRIAPA
     AHFTMGGLWS DFDQMTSIPG LFVGGEVGWG YHGANRLGAN SLLSACVDGW FTLPYSVPDY
     LAPMLGEPLL PVSDPAVAEA AESVHGRVAH LLSVGGDTAP DQFHRTLGEI LYRGCGVARS
     PEGLSTAIDE IRALREQFWS DVRVVGTGAQ FNQELERAGR VADFLELAEL MCVDALDRDE
     SCGAHFRVDH QTEQGEAVRD DDHWCFASAW ETTDAGRHIR HREPLSFHAV PLQTRNYR
//
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