ID H1XZP0_9SPHI Unreviewed; 573 AA.
AC H1XZP0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:EHQ27732.1};
GN ORFNames=Mucpa_3634 {ECO:0000313|EMBL:EHQ27732.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ27732.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ27732.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ27732.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
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; CM001403; EHQ27732.1; -; Genomic_DNA.
DR RefSeq; WP_008508289.1; NZ_CM001403.1.
DR AlphaFoldDB; H1XZP0; -.
DR STRING; 714943.Mucpa_3634; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_3_10; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000002774; Chromosome.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002774};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 573 AA; 63333 MW; 232744916B7C5D4F CRC64;
MKVSDFIAGF LEKKGVGCIF ELSGGMITHL LDSISQNTTI NIVTMHHEQS AAFAADAYGR
VTGLPGVALA TSGPGATNLL TGIGSCYFDS SPAIFITGQV NRHEQKRDKT IRQLGFQETD
IVAMAKPITK AAYLVNNAED IPYIFEEAFR IAMEGRPGPV LIDIPMDVQR AQIDTNYISS
AVEEQVNIIS EKDLKDLISD IQNAQRPLIL AGRGVKAAQC QDYFDKFIQK TKTPVITTLL
ALDTIAFDDP MRVGFIGSYG NRWANIAFGE CDLLIVLGSR LDVRQTGADT KFIENRKIYH
VDCDSCEINN RIKGCVPIVT TLDVFFKQFD IAAQNTFFNN NTNWLIHINN LKSKWPDTSE
LNPSGINPNK FMHRLAAISQ KAFAYLADVG SHQMWAAQSL QLNKGQLFLT SGGMGAMGFS
LPAAIGASIT ANKKPAVVLI GDGCMQLNIQ ELQTVVRNDL PIKIIVLNNR TLGMIRQFQD
SYFESRYQST YWGYSAPDFE KIAIAYGINA KTIDHPEEVE NAVAWLWEGE NENRPLVLQV
MIDPQTNTYP KIAFGKPITE MEPFSAPIGM EST
//
