ID A0A2Y9C6M6_9MICO Unreviewed; 579 AA.
AC A0A2Y9C6M6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SSA43283.1};
GN ORFNames=SAMN05216184_10847 {ECO:0000313|EMBL:SSA43283.1};
OS Georgenia satyanarayanai.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=860221 {ECO:0000313|EMBL:SSA43283.1, ECO:0000313|Proteomes:UP000250222};
RN [1] {ECO:0000313|EMBL:SSA43283.1, ECO:0000313|Proteomes:UP000250222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10826 {ECO:0000313|EMBL:SSA43283.1,
RC ECO:0000313|Proteomes:UP000250222};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; UETB01000008; SSA43283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9C6M6; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000250222; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; 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; 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; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:SSA43283.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000250222};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..528
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 579 AA; 61617 MW; 1330920F1BE8A330 CRC64;
MATSIAEHLV RQLAAAGVER IYGIVGDSLN PVVDAVRRTE GIEWVHVRHE EAAAFAAAGE
AEVTGRLAVC AGSAGPGNLH LINGLYDANR SRLPVLAIAS HIQSSEIGTQ FFQETHPDRL
FTEASVFSEL ITTPAQLPRV TRSAIQHAVG TPGVAVLTLP GDVADAEIDD DGQHLVPATG
AATLVPAEAD VAALAEAVNA ARKVTLFVGA GARGARAEVL ALAEQVGAPV GHSLRGKEVI
QYDNPYDVGM SGLLGYGACQ DAMEGADLLV LVGTDFPYTD FLPADVRTAQ IDVDVTHLGR
RTRLDVPVHG DVGATLRMLL PLVRRKKSRA FLKDMRKRHE KVMTKVVGAY TRKVDKHRPI
HPEYAAVRLD EAAGPDTVFT VDTGMNNVWA ARYLTPNGRR RVIGSFIHGS MANALPHAIG
AAFADPGRQV VALAGDGGLS MLLGELVTLR HYDLPVTVVV FNNASLGMVK LEMLVEGLPH
HATESPAVDY SRLAQALDIP SLRVEDPREL SGAFRDAFDR RGPVLVEVMT DPNALSIPPS
ISAGQVRGFA TSMTKQIFGG GSGEVMAMAR SNLRNVPRP
//
