ID A0A136PXT8_9ACTN Unreviewed; 645 AA.
AC A0A136PXT8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KXK63289.1};
GN Name=sdhA {ECO:0000313|EMBL:KXK63289.1};
GN ORFNames=AWW66_04100 {ECO:0000313|EMBL:KXK63289.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK63289.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK63289.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK63289.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR630664-51};
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:KXK63289.1}.
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DR EMBL; LRQV01000007; KXK63289.1; -; Genomic_DNA.
DR RefSeq; WP_067360030.1; NZ_LRQV01000007.1.
DR AlphaFoldDB; A0A136PXT8; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000070620; 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; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW FAD {ECO:0000256|PIRSR:PIRSR630664-51};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR630664-
KW 51}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070620}.
FT DOMAIN 20..441
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 497..609
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 509..536
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT BINDING 25..30
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 48..63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 425
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 440..441
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
SQ SEQUENCE 645 AA; 70683 MW; B51030E382B92B01 CRC64;
MTTTRGSEEA TTRIERHHYD VVVVGAGGAG LRAAIEARLA GKKTAIISKS LFGKAHTVMA
EGGAAAAMGN VNSRDSWQVH FRDTMRGGKF LNNVRMAELH AKESPQRIWE LETYGALFDR
TKDGKISQRN FGGHEYPRLA HVGDRTGLEL IRTLQQKIVS LQQEDRRQFG SYDARIKVFA
ETTITELILD GDRIAGAFGY YRESGEFILF EAPAVVLATG GVGRSYKVTS NSWEYTGDGH
ALALRAGATL INMEFLQFHP TGMVWPPSVK GILVTESVRG DGGVLKNSEG RRFMFDYVPD
VFRKQYAETE AEADRWYTDP DNNRRPPELL PRDEVARAIN SEVKAGRGTP AGGVFLDIAS
RRSAEEIRRR LPSMYHQFKE LADVDITKEP MEVGPTCHYV MGGVEVDPDS GAAQGHVRGL
FAAGEVSGGM HGSNRLGGNS LSDLLVFGKR AGGHAASYAD GLAARPKVAV AAVEAAVETA
LAPLQRETGE SPYTLQQDLQ AVMGDLVGII RRQDELEDAL RRLAELRARV ATVSAAGGRR
YNPGWHLALD LRNMLVVSEC TALAALERRE SRGGHTREDF PTMDPGWRRV NLVCALDGET
VSLARKPLPT MRPELIGLFD RAELAKYLTD EELAEFDART EEAGS
//
