ID B8HDF8_PSECP Unreviewed; 563 AA.
AC B8HDF8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:ACL38963.1};
GN OrderedLocusNames=Achl_0968 {ECO:0000313|EMBL:ACL38963.1};
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL38963.1, ECO:0000313|Proteomes:UP000002505};
RN [1] {ECO:0000313|EMBL:ACL38963.1, ECO:0000313|Proteomes:UP000002505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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; CP001341; ACL38963.1; -; Genomic_DNA.
DR RefSeq; WP_015936186.1; NC_011886.1.
DR AlphaFoldDB; B8HDF8; -.
DR STRING; 452863.Achl_0968; -.
DR KEGG; ach:Achl_0968; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000002505; 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; 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:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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 19..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 209..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 59311 MW; 7F079958DBF83D4E CRC64;
MIDFDPGTAA PTKGTGARNG GDLVVETLEA LGAKTVFGIP GQHALGLFDA MGRGNLQFVS
SRVENNSAFA ADGYSRATGE VGVLFLSTGP GALTSLAGLQ EAYATGVPMV VVASQIPLEG
LGARRKGMLH QLDDQKASAA NVTKSQRLIQ HASGIPSAIQ DAWTEAISSP QGPVWIEIPQ
NVLLDPIMVP PVEDALAEAA DNPPRVELVR EAVKWLQEAR RPAIIAGGGT RRGEAEKSLL
SIAEKLRAPV ICTPGGNGAF PWNHELSLQS WIEDRYMTDV LEDADVLVVI GSSLGEVTSN
YFTFEPRGRI IQIDAEPRVL ESNRPGLGIR ADAGQALAAL DEALAPADVA ADWHGSTPEE
LVKESLAKVR ARLESQDLAK ELAFMADIRE AVPADMQTFW DMTIASYWGW SCWDSREGQF
HSAQGAGGLG YGFPAAIGAA VGLETLGKPG RVLAVSGDGS SMYSISELAT AKQHNVPVTW
LIVDDGGYGI LREYMVGAFG KATATELARP DFVKLAEAFG VPAVKVAPGD VGDALKAGFA
ADGPNVVVVE TLLKMFGPTH LGD
//
