ID A0A1I2ZMN1_9GAMM Unreviewed; 598 AA.
AC A0A1I2ZMN1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SFH39077.1};
GN ORFNames=SAMN04487959_103232 {ECO:0000313|EMBL:SFH39077.1};
OS Halomonas xianhensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=442341 {ECO:0000313|EMBL:SFH39077.1, ECO:0000313|Proteomes:UP000199040};
RN [1] {ECO:0000313|EMBL:SFH39077.1, ECO:0000313|Proteomes:UP000199040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6848 {ECO:0000313|EMBL:SFH39077.1,
RC ECO:0000313|Proteomes:UP000199040};
RA de Groot N.N.;
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; FOPY01000003; SFH39077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2ZMN1; -.
DR STRING; 442341.SAMN04487959_103232; -.
DR Proteomes; UP000199040; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:SFH39077.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199040};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 169..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 65532 MW; 0F3EB459FCE617D9 CRC64;
MSELVGDFML KRLSQWNVKR IYGYPGDGSN GIMGALNRAG DQFEFIQTRH EEMAAFMACA
HAKFTGEVGV CTATSGPGAI HLLNGLYDAK KDHQPVVAIV GQQARAAMGG DYQQEVDLVS
LFKDVANEYV HMATSPAQIR HLIDRSIRIA LAERTVTVII VPNDLQSQPA VEEPPRAHGT
VHSGVGYSRP RVAPHEDDLK RAAAVLNEGE RVAILVGAGA LNATDEVIQV AEKLGAGVAK
ALLGRAALPD DLPFVTGSIG LLGTNPSWEL MENCDTLLMV GSSFPYSEFL PKEGQARGVQ
IDIDGRMVSM RYPMEVNLVG DSATTLQALL PHLKQKTDRS WREHIEKSVA QWWDVLEERA
MADADPVNPQ RVFWELSPKL PDNCILTSDS GSAANWYARD LKLRRGMMAS LSGGLATMGN
GVPYAIAAKF AHPERAVIAM VGDGAMQMNG NAELVTIAKY WQRWSDPRLI VLVLNNQDLN
QVTWEMRVME GDPKYEASQD VPDFPYADYA ELIGLKGIKV TESEALAGAW DRALNTDRPV
VLEVKTDPNI PPIPPHIKRE QAQAYMSALL HGDPDSLGTI KASFKQFARE FIPKARKH
//
