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Database: UniProt
Entry: A0A0M0BWF1_9ARCH
LinkDB: A0A0M0BWF1_9ARCH
Original site: A0A0M0BWF1_9ARCH 
ID   A0A0M0BWF1_9ARCH        Unreviewed;       568 AA.
AC   A0A0M0BWF1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KON32784.1};
DE   Flags: Fragment;
GN   ORFNames=AC477_02475 {ECO:0000313|EMBL:KON32784.1};
OS   miscellaneous Crenarchaeota group-1 archaeon SG8-32-1.
OC   Archaea; Candidatus Bathyarchaeota; MCG-1.
OX   NCBI_TaxID=1685124 {ECO:0000313|EMBL:KON32784.1, ECO:0000313|Proteomes:UP000037237};
RN   [1] {ECO:0000313|EMBL:KON32784.1, ECO:0000313|Proteomes:UP000037237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8-32-1 {ECO:0000313|EMBL:KON32784.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KON32784.1}.
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DR   EMBL; LFWU01000053; KON32784.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BWF1; -.
DR   Proteomes; UP000037237; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR   CDD; cd00730; rubredoxin; 1.
DR   CDD; cd02014; TPP_POX; 1.
DR   CDD; cd07039; TPP_PYR_POX; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR047211; POXB-like.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   InterPro; IPR018527; Rubredoxin_Fe_BS.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047212; TPP_POXB-like.
DR   InterPro; IPR047210; TPP_PYR_POXB-like.
DR   PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR   PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF57802; Rubredoxin-like; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00202; RUBREDOXIN; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:KON32784.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..44
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50903"
FT   NON_TER         568
FT                   /evidence="ECO:0000313|EMBL:KON32784.1"
SQ   SEQUENCE   568 AA;  62346 MW;  B253314C07D2E76D CRC64;
     MTKFRCTICN YVFDESKEGK KFSDLPPDWV CPVCGVPKTD FVILTEETGD QSKKLRTVSE
     VIIDQIAEWG IRYVFGVPGT STLGIVDAIR KNNKIRYIQV RHEEVAAFMA SAYGKLTGNI
     AACLSVSGPG ATNLATGLYD AALDNSPVLV LSGMVARQFI GPGSLQEIDQ HSFFEPICVF
     NKILMTEDQT TMLVTLAVKH SLLDRGVSNI GIPNDVQKLP CEKYIQPFEG RMPSLAFGVE
     DSLIEKAAKI IDLSERPVII AGYGARGQGK KLLKFAQTIS APIVTTFRSK GVIDEDHQLC
     VGIHGGTGTT SAAKLVRKSD LLVVIGSSFS QYTQLPKKRM VQIDINMKNI ARNYPVEVGL
     LGNSAILIPK LTKSVQSKQN TTYMDEIAKL KQDWNQQLQR EADASLKPIR PPYIIKVLND
     QIADDAIISL DIGENCWWFG RNFQMKKTQK MVMSGLLASM GFGLPGAMAA ALAYPERQIV
     CITGDGGFTQ IMGDFLTALK YQMPIKTFIF NNKSLGMIKQ EQKVEGYTST QTELYDFNFA
     EYSNNAGGLG IKVTEPNLLE AAVAKALA
//
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