ID J2KSU3_9SPHN Unreviewed; 594 AA.
AC J2KSU3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:EJK78216.1};
GN ORFNames=PMI04_04568 {ECO:0000313|EMBL:EJK78216.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK78216.1};
RN [1] {ECO:0000313|EMBL:EJK78216.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK78216.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EJK78216.1}.
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DR EMBL; AJVL01000097; EJK78216.1; -; Genomic_DNA.
DR RefSeq; WP_007715460.1; NZ_CP124576.1.
DR AlphaFoldDB; J2KSU3; -.
DR STRING; 1144307.PMI04_04568; -.
DR PATRIC; fig|1144307.3.peg.4166; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Ligase {ECO:0000313|EMBL:EJK78216.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 23..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 211..347
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 425..568
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 594 AA; 64835 MW; 6F23C1E1A0CFA206 CRC64;
MSYDDPKPAV NVNATDKKGT PVYKRMLDLF EAEGINTLFG IPDPNFVHMF LEAERRGWTV
VAPHHEAAAG FMAEAASRIT GKPAVAIGTL GPGIANMAPA IQCALVENSP VIFLSGQRAR
VTEQRVRRGR IQFVKQMPLF ENSVKYAASI EYADQTDEVV REGIRKAMGG TPGPVYIEYP
SHIILEELDL PAPLAPDRYR LVNQGADIDR VKEAADLIRA AKNPILLVGH AVHTSRSGAA
VKELADLMNC PVIQTSGGTS YIKGLEDRTF QYVFSKASIE AVTESDLVLA LGTELGEPVH
FGKWRYWMKN EAIRKWIYVE QDPAAIGVNR PIDVPLVGDL RGVVPQLVEA LKDTPRAPAP
GLEAFMRDGQ AELDELAAES RTKSDGTGDL PIHPARLAVE ATEAFPKDGI LIRDGGAGVI
FQWTYSQCKP NDVIWNQNFG HIGTGIPYAT GAMLADRAAT GVSRPGLLLT SDSSFMFHIA
ELEVAVRTKL PLVCVVGVDN QWGLEVGVYK RTFGQGTEET GTHWSKEVRF DKIGEGFGCH
GEYVTRAEDI KPAIARAYAS GKPGVVHVVI DPKANSEEMP KYAEFRTWYA EGTQ
//
