ID A0A0R2AUN2_9LACO Unreviewed; 553 AA.
AC A0A0R2AUN2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Alpha-ketoisovalerate decarboxylase {ECO:0000313|EMBL:KRM67641.1};
GN ORFNames=FD06_GL000793 {ECO:0000313|EMBL:KRM67641.1};
OS Apilactobacillus ozensis DSM 23829 = JCM 17196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=1423781 {ECO:0000313|EMBL:KRM67641.1, ECO:0000313|Proteomes:UP000052012};
RN [1] {ECO:0000313|EMBL:KRM67641.1, ECO:0000313|Proteomes:UP000052012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23829 {ECO:0000313|EMBL:KRM67641.1,
RC ECO:0000313|Proteomes:UP000052012};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM67641.1}.
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DR EMBL; AYYQ01000036; KRM67641.1; -; Genomic_DNA.
DR RefSeq; WP_054658057.1; NZ_BBAX01000012.1.
DR AlphaFoldDB; A0A0R2AUN2; -.
DR STRING; 1423781.FD06_GL000793; -.
DR PATRIC; fig|1423781.4.peg.822; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000052012; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000052012};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..313
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 553 AA; 60861 MW; DB6C140F44F84020 CRC64;
MSEYTVSDYL LDVIKHLGED EIFGVPGDYN LQFLDHITHR DDMKWIGNAN ELNASYVADG
YAREKGLATF VTTFGVGELS GINGLSGSIA EHVPVLEIVG APTNKVQNEG ALVHHTLGDH
EFKRFEAAHE KLGIKVTRLN KEQAINQINE TLQYIHYTKK PAYMILPSDL VNIPVNPAIK
SNIDKLFVER KFNIDKAVKQ LIQAIEKAKK PVIVVGHEIS RFNLGKQVET FASNNNIPVV
DLGLGKGAID ETFANFVGTY NGSISDDNIN EFVKSADSVI LMGAKLTDSV TGGFTQQFNP
SQTVAISIDG SSIYGENIDG ETDFVSVLNQ LADTKLNNSL PQVKVPEISD KLTASDNALT
QAFYDQAMQQ FIKRDNTLVA EQGTSFFGLA SQRLAKGANF IGQPLWGSIG YAFPAALGSQ
IANKNRRTVL STGEGSLQLT IQEFGLAFRE QIKPVIFIIE NSGYTVERVI HGMNESYNDV
PKLRYDLVPE AFGANANEYD FINVSTEKEL IDAMHKASQE PDKLVVIQAN MGMKDAPEQL
MKTAKLFEQQ NQA
//
