ID B8HJD1_PSECP Unreviewed; 575 AA.
AC B8HJD1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:ACL42529.1};
DE Flags: Precursor;
GN OrderedLocusNames=Achl_4578 {ECO:0000313|EMBL:ACL42529.1};
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OG Plasmid pACHL02 {ECO:0000313|EMBL:ACL42529.1,
OG ECO:0000313|Proteomes:UP000002505}.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL42529.1, ECO:0000313|Proteomes:UP000002505};
RN [1] {ECO:0000313|EMBL:ACL42529.1, ECO:0000313|Proteomes:UP000002505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RC PLASMID=pACHL02 {ECO:0000313|EMBL:ACL42529.1,
RC ECO:0000313|Proteomes:UP000002505};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of plasmid2 of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001343; ACL42529.1; -; Genomic_DNA.
DR RefSeq; WP_012623567.1; NC_011881.1.
DR AlphaFoldDB; B8HJD1; -.
DR KEGG; ach:Achl_4578; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_8_1_11; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000002505; Plasmid pACHL02.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
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 Plasmid {ECO:0000313|EMBL:ACL42529.1}.
FT DOMAIN 12..392
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 447..535
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 575 AA; 63009 MW; 0CE4522108842D48 CRC64;
MNIQEKRITT AVLVIGTGGS GLRAAIELAE RGVDVIAVGK RPKADAHTSL AAGGINAALA
TMDPEDTWQQ HAADTIRESY LLANPLTVQI VAEGAERGIG DLERYGMNFA REENGAISQR
FFGAHKFRRT AFAGDYTGLE IQRTLIRRAE QLRVPILDTI YITKLLVREN TIFGAYGFDL
EDGTRYVIHA DAVILAAGGH NRIWRRSSSR RDENTGDSFR LAVEAGGRIR DPELVQFHPS
GIIEPESAAG TLVSEAARGE GGILRNARGE RFMERYDAER MELSTRDRVA LAAYTEIKEG
RGTANGGVWL DVSHLPRKVI MERLPRVYQT LLDVQMLDIT KDPIEIAPTA HYSMGGVWVR
PEDHGTDVDG LYAIGEAASG LHGANRLGGN SLIELLVFGR IVGEAAAKYS NQLESQRRSL
EAIVEARSEV DALLACQGSE NVRALQRAVR DTMTEHAGVV RSEEGLIAGL EELDSTEDRL
EHLGIHPDIA GFQDLAHAFD LKSSLLAARA TLEAALERRE SRGCHNRSDF PDQDESLQVN
FVWSPGRLDR EAIPPIPDEI AELMQDVSTA GKLVE
//