ID S2VZU0_9ACTN Unreviewed; 683 AA.
AC S2VZU0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Succinate dehydrogenase or fumarate reductase, flavoprotein subunit {ECO:0000313|EMBL:EPD32391.1};
GN ORFNames=HMPREF9306_01961 {ECO:0000313|EMBL:EPD32391.1};
OS Propionimicrobium lymphophilum ACS-093-V-SCH5.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionimicrobium.
OX NCBI_TaxID=883161 {ECO:0000313|EMBL:EPD32391.1, ECO:0000313|Proteomes:UP000014417};
RN [1] {ECO:0000313|EMBL:EPD32391.1, ECO:0000313|Proteomes:UP000014417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-093-V-SCH5 {ECO:0000313|EMBL:EPD32391.1,
RC ECO:0000313|Proteomes:UP000014417};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Propionimicrobium lymphophilum ACS-093-V-SCH5.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPD32391.1}.
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DR EMBL; AGZR01000009; EPD32391.1; -; Genomic_DNA.
DR RefSeq; WP_016456766.1; NZ_KE150269.1.
DR AlphaFoldDB; S2VZU0; -.
DR STRING; 883161.HMPREF9306_01961; -.
DR PATRIC; fig|883161.3.peg.1950; -.
DR HOGENOM; CLU_014312_7_0_11; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000014417; Unassembled WGS sequence.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; 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:UP000014417}.
FT DOMAIN 82..487
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 549..682
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 32..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 683 AA; 75527 MW; 77A2AA1E4D5B77F8 CRC64;
MSFLKKLQAV FVQAETLETE PDKPVTAKRA LNVSVTPEAS KQRSSHEGLD AHVPNGDPRT
AWQRRKSEYK LVNPANRKKM KIIVVGTGLA GSGAAAALGE LGYQVDVFTF HDSPRRAHSV
AAQGGINAAR ARKVDGDSIK RFVVDTVKGG DFRAREADVV RLAEESIRVI DHMQAIGAPF
AREYGGQLAT RSFGGVQVSR TYYTRGQTGQ QLQINSAQAL QRQVARGTVK LHTRTEMLDL
IVADGKAQGI VTRDLVSGEV KTWTAHAVIL ATGGYGSVFF HSTLAMNSNA SATWRAHKRG
AYFASPAFIQ FHPTALPVSS YWQSKTTLMS ESLRNDGRIW VPKDADDTRA PNDIPEADRD
YYLERRYPAY GNLTPRDVAS RAARVEIEAG RGVGPLKNSV YLDFRDAIAS LGKDVIAERY
GNLFDMYRDA TGEDPYVQPM RIAPGAHFSM GGLWTDFDQM TSIPGLFVGG EAGNNYHGAN
RLGANSLLSA CVDGWFTLPL SVPNYLAGLV GQDVLSQDAP EVTQAKQETV SRIDKLVSNP
GKTRPATFHR RLGEILYQHC GVSRNEASLR EGLTKVRILR DEFHRDVLVM GEDNRLNQEL
EKAGRVSDFL ELAELIILDA LERDESCGAH YREEYALPDG EAARKDEQWC NVSAWETTPN
GNHIRHSEEL RFELVPLQVR NYR
//
