ID A0A2S6N604_RHOGL Unreviewed; 549 AA.
AC A0A2S6N604;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Indolepyruvate/phenylpyruvate decarboxylase {ECO:0000313|EMBL:PPQ30032.1};
GN ORFNames=CCS01_20245 {ECO:0000313|EMBL:PPQ30032.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ30032.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ30032.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ30032.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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:PPQ30032.1}.
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DR EMBL; NHRY01000218; PPQ30032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6N604; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
DR GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:InterPro.
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; IPR017765; IPDC.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR NCBIfam; TIGR03394; indol_phenyl_DC; 1.
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.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW Pyruvate {ECO:0000313|EMBL:PPQ30032.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239724};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..516
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 549 AA; 58156 MW; A9E32C35588AEDB9 CRC64;
MPALGQVLLD ALKTHGAGEI FGIPGDFVLP FCRMIEDSAT LPFYTLSHEP AVGFAADAAA
RFHGGLSVAV VTWGAGALNL VNATAGAYAE RVPLVVISGA PGLHERASGW QLHHMARTLD
TQMRIFTEIT CAQANLLDPS AAAAEIARVL RAAREYSLPV YLELPRDLVT AGAASVTPLP
PRRADPEALA ECAGEILARL AAAKQPVMLV DVELRRYGVE RAAAALARRL GLPVVTTFMG
RGLLSQGPDV IAGTYLGAAG QPAITRLVED SDTPLLLGVI LSDTNFAVSE RKIDMRRAIL
ATNREVRIGH HVYPDVPLAD LLDALLARAA PAQRAGQQFP PPRYAHGLAA DAAPLTPSDI
ACAVNDLFAA HGPMPIACDM GDCLFTAMEI ANSRLVAPGY YAGMGYGVPA GLGVAVATGE
RPLILVGDGA FQMTGFELGN CRRYGWDPIV IVFNNASWEM LRVFQPESRF NDLDDWGFAR
LAEALGGRGM RATTRAELAA ALAEAHATRG RFCLVEAMLP RGTTSDTLAR FVAGFKAARL
RLANDGPGQ
//
