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
//