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
//