ID K9RG62_9CYAN Unreviewed; 547 AA.
AC K9RG62;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:AFY56491.1};
GN ORFNames=Riv7116_4053 {ECO:0000313|EMBL:AFY56491.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY56491.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY56491.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY56491.1,
RC ECO:0000313|Proteomes:UP000010380};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) 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; CP003549; AFY56491.1; -; Genomic_DNA.
DR RefSeq; WP_015120054.1; NC_019678.1.
DR AlphaFoldDB; K9RG62; -.
DR STRING; 373994.Riv7116_4053; -.
DR KEGG; riv:Riv7116_4053; -.
DR PATRIC; fig|373994.3.peg.4317; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_3; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02010; TPP_ALS; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:AFY56491.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010380};
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 186..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 547 AA; 59603 MW; EB3AE32DD006299B CRC64;
MDTAELLVKC LENEGVQYVF GLPGEENLHV LEALKKSSIQ FITTRHEQGA AFMADVYGRL
TGKAGVCLST LGPGATNLMT GVADANLDGA PLVAITGQVG TDRMHIESHQ YLDLVAMFAP
VTKWNKQIVR PSITPEIVRK AFKRAQREKP GAVHIDLPEN IAAMPVEGKP LGKDNVEKSF
ASFATIRAAA AAISQATNPI ILVGNGAIRA KASDAVTQFA TELNIPVANT FMGKGIIPYT
HPLALWTVGL QQRDFSICGF DNTDLVIAIG YDLIEFSPKK WNPNGEIPII HIASKLAEID
SSYIPEVEVV GDITDSLNEI LKVANRHDKA APYAIKLREN IRADYENYAD DDAFPMKPQK
LIYDLRQVMG PEDIVISDVG AHKMWIARHY HCHSPNTCLI SNGFAAMGIA IPGALAAKLV
HPNRKVVAVS GDGGFMMNCQ ELETALRVGT PFVTLIFNDG GYGLIEWKQE NQFGEGKASF
IKFGNPDFVK FAESMGLKGY RVEAATDFVP MLKEALAQDV PAVIDCRVDY RENMRFTKKA
GALNCAV
//
