ID G4HHJ5_9BACL Unreviewed; 541 AA.
AC G4HHJ5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:EHB63571.1};
GN ORFNames=PaelaDRAFT_3456 {ECO:0000313|EMBL:EHB63571.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB63571.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB63571.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB63571.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) 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; AGIP01000007; EHB63571.1; -; Genomic_DNA.
DR RefSeq; WP_007130621.1; NZ_AGIP01000007.1.
DR AlphaFoldDB; G4HHJ5; -.
DR STRING; 743719.PaelaDRAFT_3456; -.
DR PATRIC; fig|743719.3.peg.3502; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000003891; 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; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 375..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 541 AA; 58510 MW; 79AAC1DD0129E047 CRC64;
MNIAEAVLKY LRNVGVDCIF GIPAGIIGPI YDALIDVDIK PIITKNEAGA AYMAARYASN
SGKLAVCAGA GAVGVGNMMN GIADAMRAKA PLLVITGYVN RWQIGKGAIQ EMDAQDIVRP
ITKYSNTVMN EADVLAELDK AVRIALTPPC GPVHISVPID VQRMEAPALL PAAPEPSALQ
RIRPNPDEME RAAALLNEAE RGIIMVGRGG RSSAEAIMRL SERLQWPIIT TPSAKGIIPA
EFPLNLGNYG FSSTDAAMEY VTSSKATCIL ILGTSLGESS TCNFNDVLVD GRKVIHVDRD
AKELGKVFRT DAAVVADLRD AVPYFAEHVS PSSASFKKPF PLNEAYEPNH TGLSLRLFLE
KLSQVMPADT RYVCDIGEFT NFVLKYLEVP AGGDFEINLN YGAMGSAMAG GPGLYLADST
RPVAVIAGDG SFFMNGTEVL TAKEYGLPII YFIINNAMLS YVERGQKFLY NRTIPDYKQE
RISIADMMRI AGIRAMSVDR LEDMEDIPGF LREMTGPCII EVNTDGSEPA PILDRLKALK
K
//
