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Database: UniProt
Entry: E4MTW8_CAPOC
LinkDB: E4MTW8_CAPOC
Original site: E4MTW8_CAPOC 
ID   E4MTW8_CAPOC            Unreviewed;       603 AA.
AC   E4MTW8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Thiamine pyrophosphate enzyme, N-terminal TPP binding domain protein {ECO:0000313|EMBL:EFS96924.1};
GN   Name=poxB {ECO:0000313|EMBL:EFS96924.1};
GN   ORFNames=HMPREF1977_1840 {ECO:0000313|EMBL:EFS96924.1};
OS   Capnocytophaga ochracea F0287.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=873517 {ECO:0000313|EMBL:EFS96924.1, ECO:0000313|Proteomes:UP000005391};
RN   [1] {ECO:0000313|EMBL:EFS96924.1, ECO:0000313|Proteomes:UP000005391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0287 {ECO:0000313|EMBL:EFS96924.1,
RC   ECO:0000313|Proteomes:UP000005391};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (OCT-2010) 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:EFS96924.1}.
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DR   EMBL; AEOH01000043; EFS96924.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4MTW8; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_0_10; -.
DR   Proteomes; UP000005391; 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; 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.
PE   3: Inferred from homology;
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          26..136
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          223..343
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..551
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   603 AA;  66457 MW;  FB69380484F1059A CRC64;
     MRLKIVLIGI IFAYKKPLII KHMSKNVSDQ LVEMLVQAGV KRVYAITGDS LNPVNDAIRR
     DGRLEWIHVR HEESAAYAAS MDAELNGIGC CMGSSGPGHV HLINGLYDAN RSGNPVIAIA
     STCATHKFGT HWFQETNPFL LFQDCSKYVY VANTPKQFTT MMQRAIQTAI NEKGVAVLGL
     PGDVAGADLE EVPSATQTFL AKPVVRPSDS ELDKLSAVLN DAKNKKIALY CGHGCQYAVK
     EVEQLAETLK APIVASFRGK IFFDRTDSPY IAGMNGLLGH RSGYDACAKA DVLVMLGIDF
     PYAEFLPKKN TIIQIDERPD IIGRRAKVDY GFAGDVKDTI TALLPKLTPR TDDSFLKDIH
     KEYLELEKSL DDYTKKKTEE NQIDPEYAAK LLDKYAANDA IFTVDTGMNV VWAARFIKGT
     GKRYLTGSFN HGSMANALPM AIGAAASSKG RQVVAMCGDG GLSMLLGDLA TLMQYQYPVK
     IFVFNNRSLA MVKLEMEVSG YLDWQTNMVN PPFDKLADLM NIKGYEVRKT EDLEATVKAA
     FEHDGPTLVN IYTNRDTLAM PPHITFEQMK GFATNIIKKI GQGDFAEAKG SIANSMKHIK
     DVF
//
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