ID Z4WUQ4_9PORP Unreviewed; 685 AA.
AC Z4WUQ4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Dehydrogenase E1 component {ECO:0000313|EMBL:EWC91495.1};
GN ORFNames=HMPREF0636_0438 {ECO:0000313|EMBL:EWC91495.1};
OS Porphyromonas catoniae ATCC 51270.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=887901 {ECO:0000313|EMBL:EWC91495.1, ECO:0000313|Proteomes:UP000023482};
RN [1] {ECO:0000313|EMBL:EWC91495.1, ECO:0000313|Proteomes:UP000023482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51270 {ECO:0000313|EMBL:EWC91495.1,
RC ECO:0000313|Proteomes:UP000023482};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EWC91495.1}.
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DR EMBL; JDFF01000024; EWC91495.1; -; Genomic_DNA.
DR RefSeq; WP_044169401.1; NZ_JDFF01000024.1.
DR AlphaFoldDB; Z4WUQ4; -.
DR PATRIC; fig|887901.3.peg.1445; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000023482; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000023482}.
FT DOMAIN 357..536
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 685 AA; 76395 MW; BD6194592F18919D CRC64;
MSIQKNYIKK RYGIKITDKD TLRRWYHLLY LGRLLDEKAP SYLLQSIGWQ FHASNAGHDG
IQLAIGQVFQ RGKDHLFLYY RDLLAALSAG MTVEEMILNG ISKATDPTSG GRHMSDHYAK
IEWGIHNISS CVAAHDSQAV GLARALDYYG VDGVAIASHG ESSASEGYVF EAINGAARER
LPVIFVLQSN GYGISVPTHE QTANPRVGEN YAGIRHLKTL FCNGKDIFDS MNTMAAAREY
AVEHRTPVVV TAECVRIGAH SNSDKHTLYR SDEEIERAKA ADPLPKFRRM LLRYNRFTEE
ELQQIEHEAQ EELKIANRNA MKAPEPSADT VLDYVIGEAY PGDKYGLGIP DGTGEELTLV
QALNKTLKQE FRHNPDTFLW GQDVANKDKG GVFNVTKGML QEFGHKRVFN APIAEDYIVG
TANGMSRFSD KIRIVIEGAE FADYFWPAME QFVNSTHDFW RSNGQFSPNI TIRLSSGGYI
QGGLYHSQNI EAVLTTFPGA RVVYPCFADD AAGLLRTAMR SRGVTVFMEP KAQYNSAEST
AIIPEDFEVP FGKARIRREG TDVTLITYGN TLHLSLNVAE RIQKELGKSI EVIDLRSLAP
WDEETVYASI RKTSKALIVH EDRVFGGFGA ELAASIAKKA FRDLDAPIYR VGSLSTPVGF
HKCFELATLP SEEKIYTTAK ELIEY
//
