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Database: UniProt
Entry: M9RK27_9RHOB
LinkDB: M9RK27_9RHOB
Original site: M9RK27_9RHOB 
ID   M9RK27_9RHOB            Unreviewed;       184 AA.
AC   M9RK27;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Putative sulfopyruvate decarboxylase subunit beta {ECO:0000313|EMBL:AGI70190.1};
GN   ORFNames=OAN307_c48450 {ECO:0000313|EMBL:AGI70190.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI70190.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI70190.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI70190.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
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DR   EMBL; CP003740; AGI70190.1; -; Genomic_DNA.
DR   RefSeq; WP_015502075.1; NC_020911.1.
DR   AlphaFoldDB; M9RK27; -.
DR   STRING; 391626.OAN307_c48450; -.
DR   KEGG; oat:OAN307_c48450; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_117492_1_0_5; -.
DR   OrthoDB; 8218035at2; -.
DR   Proteomes; UP000005307; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03372; TPP_ComE; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR022494; Sulfopyruvate_deCO2ase_bsu.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR03846; sulfopy_beta; 1.
DR   PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:AGI70190.1}.
FT   DOMAIN          40..155
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   184 AA;  19665 MW;  7516EC8B8F1A8976 CRC64;
     MIRSEILRDI APILRDQLVV CNIGLPSQEL HMIDDQPSNF YMLGTMGLAS SIGLGLALAQ
     DKTVISIDGD GSVLTNLGTL PTIANNVTDN YILMIIDNGS YGSTGDQPTY AGMKTKLEKV
     AEACGCENVV VCKDVDTGEV LQAALDSKKM TVIVVKCDSG NIKLPVITMD PVVIRDRFMK
     AVAS
//
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