ID D7A484_STAND Unreviewed; 563 AA.
AC D7A484;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding protein {ECO:0000313|EMBL:ADH87904.1};
GN OrderedLocusNames=Snov_0571 {ECO:0000313|EMBL:ADH87904.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Starkeya.
OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87904.1, ECO:0000313|Proteomes:UP000006633};
RN [1] {ECO:0000313|EMBL:ADH87904.1, ECO:0000313|Proteomes:UP000006633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP002026; ADH87904.1; -; Genomic_DNA.
DR RefSeq; WP_013165409.1; NC_014217.1.
DR AlphaFoldDB; D7A484; -.
DR STRING; 639283.Snov_0571; -.
DR KEGG; sno:Snov_0571; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_5; -.
DR OMA; GFPIKPQ; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000006633; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 11..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 60364 MW; C3FCA0EF536F949F CRC64;
MNAAHSPSAR TGAHLLVDAL IANGVTRAFG VPGESYLDVL DALSDTEVDF VVCRQEGGAA
MMAEASGKLT GRPGICFVTR GPGATNASAG VHIAQQDSTP MILFVGQISR SMRGREAFQE
VDYRAVFGTL AKWAVEIDEA ARIPEIIARA FRVAMQGRPG PVVIALPEDV LSEYADVPDA
PPVEPAETWP GLTDMMRLQK LLWEAERPIM IVGGTRWNPK AVAALVRFAE RCDLPVAVSF
RRQMLFPADH PCYAGDVGLG INPKLVGRLK EADLVIVAGG RLGEVPSQGY SLFPIPDPGV
PFVHVHAEAD ELGRVYQPTL AINASNAAFA AALEGVQPPH VVPWDDWREA VRDDYLAWTE
EPPANPGAVQ MATLVRYLRA LPDDTTICNG AGNFATWVHR FHRFRAYGTQ LAPTSGSMGY
GFPAAVAAKR AHPERTVVAV CGDGDFLMTG QEFATAVQYG IPVIAVVIDN GMYGTIRMHQ
EREFPTRVYG TALKNPDFAA YARAFGGFGV TVETDAEFTP ALEAALAAGL PAVVHVKLDP
EAITPTMTLS ALREKALADR SVG
//