ID A0A402BHH8_9CHLR Unreviewed; 556 AA.
AC A0A402BHH8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Putative 2-ketoarginine decarboxylase AruI {ECO:0000313|EMBL:GCE30750.1};
GN Name=aruI {ECO:0000313|EMBL:GCE30750.1};
GN ORFNames=KDA_62340 {ECO:0000313|EMBL:GCE30750.1};
OS Dictyobacter alpinus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=2014873 {ECO:0000313|EMBL:GCE30750.1, ECO:0000313|Proteomes:UP000287171};
RN [1] {ECO:0000313|Proteomes:UP000287171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno16 {ECO:0000313|Proteomes:UP000287171};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:GCE30750.1}.
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DR EMBL; BIFT01000002; GCE30750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402BHH8; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000287171; Unassembled WGS sequence.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000287171};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 556 AA; 60359 MW; DFA4E20388776AF8 CRC64;
MTNRQHLTGA QAVTAALRAY NVDTIFGIPG VHTLPIYDAI YHEPGLRHIL ARHEQGAGFM
AEGYARATGR PGVVCTITGP GVTNVTTPAA SAYADSIPLL IISSSLSRAS QGRARGELHE
VKDQLGVMQS LVGWTRAVNY VEEIPEAIHD AFRMMQQGRP RGAYIQIPYD LLTQSADVDI
TIAGPVERPL PSIEAMANAV EVLRESRRPL IIAGAGVTAS NANKQLLQLA ELLQAPVLLG
SKSHDVLPTQ HPLVLATNDN LPLELDAFIA TRDAVLVVGS KLGAERTADR RLPLPEKLIH
IDIDPMEIGH NYRTQIGIVS DAKVALEALY KFLKEFPQEC RAPYSALDDL REALYLHTVE
YQGENFRMLE GVSAALEQMP EDTVVVADMT MLGYAAAQYL PMRHPRTFIH PAELCTIGSG
LPLAIGAQAG LPGRPVIALC GDGGFLLNSS ELATASQEKL PVIVVIFNDA TFTRVKTDQH
QNYDSRYIAT DLLAPDYVAL ARAFHAESMR VTTPEELSTA IQQSANHAGP TVIEVPLLVR
PWQKEQSTEH TAITLA
//
