ID A0A330LA44_9BACT Unreviewed; 551 AA.
AC A0A330LA44;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Putative Pyruvate decarboxylase {ECO:0000313|EMBL:SPP65969.1};
DE EC=4.1.1.1 {ECO:0000313|EMBL:SPP65969.1};
GN ORFNames=NITLEN_50009 {ECO:0000313|EMBL:SPP65969.1};
OS Nitrospira lenta.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1436998 {ECO:0000313|EMBL:SPP65969.1, ECO:0000313|Proteomes:UP000248168};
RN [1] {ECO:0000313|Proteomes:UP000248168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucker S., Sakoula D.;
RL Submitted (APR-2018) 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}.
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DR EMBL; OUNR01000018; SPP65969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A330LA44; -.
DR InParanoid; A0A330LA44; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000248168; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; 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; 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; 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, ECO:0000313|EMBL:SPP65969.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW Pyruvate {ECO:0000313|EMBL:SPP65969.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248168};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..110
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 551 AA; 59644 MW; 2DC264CDACD7A187 CRC64;
MNHPATIGTA VLDRLHGLGV RHIFGIPGDY VLSLYQLIEA SPIKHIGTTR EDCAGFAADA
YARINGIGAA CVTYCVGGLN TVNAIACAYA ERSPVVLLTG SPGLSERTRT PYMHHMVRDF
STQRDVFEQM TVAAITLDDP LTAEREMDRA FAALLRYRRP IYIEIPRDMV HSPLHGSGKP
ACIDEALSDA AALAEAIGEV RMMLSAAHRP AILVGAEVGR FGLHDDLAKL VERLNIPIAS
TLLGKSVIRE DHPLYVGVYG GLIGRDEVQQ FINESDCLLI LGSILSDVED VDARSPLMTE
GRTIHATADR IAVKHHRYEA IRFQDFVRGL GEAPLPSFPS RTLPAPPSPA GPALDPAGPI
TLRGLFGHLD TILNEQTLVI ADVGESLFAA ADLHVHRRFE FLSPAYYTSM GFAIPAALGA
SCADPTLRPI VLVGDGAFQM TGTELSSCVR YGQAPIVIIL NNRGYSTERE ILEGPFNDIH
EWQYERICDL VGGGVGSRVT TQQGFEQRIA AALADSTQVH VLNVLLNPAD RSPGMVRLAR
RLGKKLSTDK P
//
