ID A3K365_9RHOB Unreviewed; 570 AA.
AC A3K365;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Pyruvate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:EBA08624.1};
GN ORFNames=SSE37_17468 {ECO:0000313|EMBL:EBA08624.1};
OS Sagittula stellata E-37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sagittula.
OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08624.1, ECO:0000313|Proteomes:UP000005713};
RN [1] {ECO:0000313|EMBL:EBA08624.1, ECO:0000313|Proteomes:UP000005713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-37 {ECO:0000313|EMBL:EBA08624.1,
RC ECO:0000313|Proteomes:UP000005713};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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:EBA08624.1}.
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DR EMBL; AAYA01000005; EBA08624.1; -; Genomic_DNA.
DR RefSeq; WP_005858647.1; NZ_AAYA01000005.1.
DR AlphaFoldDB; A3K365; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000005713; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd02014; TPP_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 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:EBA08624.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005713};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..316
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 377..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 570 AA; 61592 MW; F1ACAE92B498F870 CRC64;
MAKVAEIVVD ALLEAGAKRC WGIVGDTINH FTDAVRKSDL CWVHVRHEEA GGLAAGGEAY
FTGELVVCAG TCGPGTLHFV NGMFESHRNG APVVLIASDV ARAETGLGFP QELDQRKIYE
QYSVFCEYIS HPDQARRITV QAAQAALTKG GVAVVIVNGD MFEEDSKDDL PWSVHRPKSH
LRPVDAELDA LAEKLNAAGT VTLYAGIGAR DAKPQLVALA QKLAAPIAHT SRSKEFIEPD
NPYNIGMIGI LGNKAGVEAI DAADVMLCLG TDFAYTQFYP GQEKIVQIDR DPTHIGRRAP
VGMGLVGDVG ATIDALLDRL KQKNDKSHLE AARKQWKKDL DGYADEAEES DPSLIHPQFV
THTLDRLAAP DAIFTADGGS PMVWLLRHLT ANGQRNFLTS LLHGTMANAY PQAMGAAAAY
PDRQVISMSG DGGMTMLMGD LLTLKQEKLP VKILIYNNGS LGFVEMEQRV EGLLDSYTGL
ENPDFAKLAE VCGLKGWRVE NADDLEGAMA EWLAADGPAV LDVRVNRVEL VMPPKVEAGQ
VASTALFGMK AVLDGRAREV ISLLRDNFLR
//
