ID A0A0R2XGX5_9BACT Unreviewed; 556 AA.
AC A0A0R2XGX5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Indolepyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABS33_03540 {ECO:0000313|EMBL:KRP33740.1};
OS Verrucomicrobia subdivision 6 bacterium BACL9 MAG-120924-bin69.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Verrucomicrobia subdivision 6.
OX NCBI_TaxID=1655635 {ECO:0000313|EMBL:KRP33740.1, ECO:0000313|Proteomes:UP000051220};
RN [1] {ECO:0000313|EMBL:KRP33740.1, ECO:0000313|Proteomes:UP000051220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL9 MAG-120924-bin69 {ECO:0000313|EMBL:KRP33740.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Evidence={ECO:0000256|ARBA:ARBA00001920};
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:KRP33740.1}.
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DR EMBL; LIDN01000089; KRP33740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2XGX5; -.
DR Proteomes; UP000051220; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase 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; cd02005; TPP_PDC_IPDC; 1.
DR CDD; cd07038; TPP_PYR_PDC_IPDC_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; IPR012110; PDC/IPDC-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF036565; Pyruvt_ip_decrb; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 411..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 556 AA; 60608 MW; 71C5D3166E71097A CRC64;
MSKNLTVVEY VINRLADLGI DRAFGVPGDY SFPIDDAIEF SSRMKWVVCA NELNASYAAD
GYARRRGAAL LTTTYAVGEL SAVNGVMGAK AHRVPIFHVV GAPSTRIQRA GMITHHTLGD
GVYGNFFDIS AACCGVSAKI TPDNVITEME RVIHEAFRLS QPAYIQIPED YAVMPVQGIP
VKGKRLPHVF RGKSNPIEVK AAVRAILARL KKAKRPIAMP SFQVKRYHAQ PQLLSLLKRT
GLPFTLTSMD KGVVDESHPN YLGLFAGKDS APASAGKAAL SADLILCVGE VLEEDFNVGS
WSALLDPARK VILGPDYVKV GDQYFTSCML PDVLAALARS APRVKRAKHP APKFLPMVGQ
PHDPISSAAL YPRLQRFLRE GDNLVVEGGS CMFPCASLLL PKGVSYEGQI LWASIGWATP
TTLGVALAEP KRRTIMVSGD GAHQLTANEI GVMGRYGINP ILIVLNNGIY GVEDVLSERG
HVYDDLAGWN YHTLPAAMGC RDWFCTRIET VGDLESALEE ARNHRGACYL EVMIPETESQ
PLSKKTINRI YKTYAK
//
