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Database: UniProt
Entry: A0A0Q9KXK8_9MICC
LinkDB: A0A0Q9KXK8_9MICC
Original site: A0A0Q9KXK8_9MICC 
ID   A0A0Q9KXK8_9MICC        Unreviewed;       579 AA.
AC   A0A0Q9KXK8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KRE46064.1};
GN   ORFNames=ASG92_11595 {ECO:0000313|EMBL:KRE46064.1};
OS   Arthrobacter sp. Soil736.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE46064.1, ECO:0000313|Proteomes:UP000051775};
RN   [1] {ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE46064.1, ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|EMBL:KRE46064.1,
RC   ECO:0000313|Proteomes:UP000051775};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KRE46064.1}.
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DR   EMBL; LMSB01000066; KRE46064.1; -; Genomic_DNA.
DR   RefSeq; WP_056635184.1; NZ_LMSB01000066.1.
DR   AlphaFoldDB; A0A0Q9KXK8; -.
DR   STRING; 1736395.ASG92_11595; -.
DR   OrthoDB; 9813348at2; -.
DR   Proteomes; UP000051775; Unassembled WGS sequence.
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; 2.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding 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}.
FT   DOMAIN          12..545
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   579 AA;  61274 MW;  31FC4B3B808F1EEB CRC64;
     MSRTGTRTTV CDVLVIGSGV AGMAAALKAA SQGLSVIVAE KEQYFGGTTA ISAGWAWVPG
     NKQGVAQGDT REEAETYLKN LAPETFNEAG VRDFLDTVPE AISFFENETE VKFTYPEKSP
     DYQMDLPGAK LSGRAILPQD VDARVLGDKR LLMQPYMSSY TVFGYMPQVG PDINEFFHVN
     QSVKSFVYVA KKLLRTWADA ARYRRPVLRS NGNALMTRMV KSADDLGVRL WKSSPALSLT
     RDDAGTVTGA VIGGQHAATV TARLGVILAA GGFSGNKELR QQYFPHDADG DDHFTPTVGH
     GGDAATLAIS AGGHIDDSVF SVGSWAPVTV FKYLNGKQRL FPHLRAIGLP GLIAVDRHGK
     RFGNEALSYH DFGGAMIGHN KDEDKTFGYV IGDAKTMHKY GIGYAKPWPM PRGYFYKTGY
     LVKGDTLAEL AGKLGIDAEG LKATVADFNP AAERGEDPAF GRGSTLYNHF RGDLEHTPNP
     NLAPVGKGPY YAAKIQMGDL GTFAGVGVNE GSEVVTAEGT AIPGLLAVGA AAVSVFGGGY
     PGYGSHIGPA LVFGYRAGRD IAGLAAARGA GRAATVAAG
//
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