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Database: UniProt
Entry: A0A1H9RCE8_9BACI
LinkDB: A0A1H9RCE8_9BACI
Original site: A0A1H9RCE8_9BACI 
ID   A0A1H9RCE8_9BACI        Unreviewed;       502 AA.
AC   A0A1H9RCE8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Tricarballylate dehydrogenase {ECO:0000313|EMBL:SER70601.1};
GN   ORFNames=SAMN05518872_101695 {ECO:0000313|EMBL:SER70601.1};
OS   Psychrobacillus sp. OK032.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1884358 {ECO:0000313|EMBL:SER70601.1, ECO:0000313|Proteomes:UP000199084};
RN   [1] {ECO:0000313|EMBL:SER70601.1, ECO:0000313|Proteomes:UP000199084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK032 {ECO:0000313|EMBL:SER70601.1,
RC   ECO:0000313|Proteomes:UP000199084};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOGY01000001; SER70601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9RCE8; -.
DR   STRING; 1884358.SAMN05518872_101695; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000199084; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding 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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING 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          8..473
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   502 AA;  55350 MW;  6F9C12166D714212 CRC64;
     MSHTQSYDVV VVGAGNAALC SAIAAKEGGA SVLVLERGPV EKRGGNSFFT DGAIRVAYNN
     LDAIRKVIPE LTDEEAEMIV MPEYGEKDYY DDLMRVTGGK SDAGLAKQLV SKSYETITWM
     RDQGIKFELN YDNQSFIQDG KRHFWGGLPI KTEDKGVGLM KQLFARVKEL GIDIWYEARA
     VKLIKENDQI TGIVVEKDND TITVNTGSVI LACGSFEANK KLRSEHIGEE WEAAIVRGTE
     FNTGDGIFMA LEVGAQKFGE WSGCHSIGTD SNAPIVGDFT KPGDIFKKHS YPYSIMLNNE
     GKRFVDEGAD LRNYTYAKYG REILKQPGHV AYQIYDAQVR PMLRKEYDLE EATFYQADTL
     EELANLLPVD KKQFLETIEE YNKAVQEGDY KPAEKDGKGT IGITPSKSNW ALRIEKSPFY
     AFPVTCGITF SFGGLHVDPL GEVLDKEEQP IKGLFAAGEM IGGIFYENYP GGSGLMSGAV
     YGKLAGTSAA QYILGKSAEL VN
//
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