ID J9DKB8_9STAP Unreviewed; 580 AA.
AC J9DKB8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EJX18496.1};
GN ORFNames=SOJ_06740 {ECO:0000313|EMBL:EJX18496.1};
OS Staphylococcus sp. OJ82.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1202667 {ECO:0000313|EMBL:EJX18496.1, ECO:0000313|Proteomes:UP000006164};
RN [1] {ECO:0000313|EMBL:EJX18496.1, ECO:0000313|Proteomes:UP000006164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OJ82 {ECO:0000313|EMBL:EJX18496.1,
RC ECO:0000313|Proteomes:UP000006164};
RX PubMed=23105083; DOI=10.1128/JB.01653-12;
RA Sung J.S., Chun J., Choi S., Park W.;
RT "Genome Sequence of the Halotolerant Staphylococcus sp. Strain OJ82,
RT Isolated from Korean Traditional Salt-Fermented Seafood.";
RL J. Bacteriol. 194:6353-6354(2012).
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:EJX18496.1}.
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DR EMBL; ALPU01000003; EJX18496.1; -; Genomic_DNA.
DR RefSeq; WP_002506655.1; NZ_ALPU01000003.1.
DR AlphaFoldDB; J9DKB8; -.
DR GeneID; 69844929; -.
DR PATRIC; fig|1202667.3.peg.671; -.
DR Proteomes; UP000006164; 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:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-KW.
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 Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428};
KW Pyruvate {ECO:0000313|EMBL:EJX18496.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 63833 MW; AD7E0914AE2FC2B9 CRC64;
MAKIKANEAL VKALQAWDID HLYGIPGDSI DAVVDSLRTV RNNIKFVNVR HEEVASLTAS
SYTKVTGKIG VALSIGGPGV IHLLNGMYDA KMDNVPQLIL AGQTDSTALG TKAFQETDIS
KLVDDVSVYN RQISENDKDI FGIVNEAIRT AYEKKGVAVL ILPNNLLTNK VKDTTNTKVD
TAPPARVTPK PRSIKKATKL INKSKRPVVL VGMGAKHAKD ELLQFIEAVK IPSIITLPAK
GLLADAHPYN IGNLGKIGTK TSYQTIQDAD LLIMIGTNYP YVDYLPKKNI KAIQIDNNAE
NIGHRFDVNV GIVGDSKLSL LQLTDSVKHV SERDFLTKTL ERKATWDAWM AKDLEDNSKP
IRPERLMDAI NQVRTDDAIF SIDVGTSTVW STRYLNLTVN NKFIVSSWLG TMGCALPGAI
AAKTAYPNRQ VVGIAGDGAF QMVMQDFATA VQYDLPMTFF VLNNQQLSFI KYEQQAAGEL
EYAINFTDID YAKFAESCGG VGYTLTDPNR IDEVVEDAMS QDRPTIVNVY VDETAAPLPG
KIVMDEAMNY GKWAFRSITE DGKLDLEELP PMSTAVKRFF
//
