GenomeNet

Database: UniProt
Entry: A0A0K2G7V5_NITMO
LinkDB: A0A0K2G7V5_NITMO
Original site: A0A0K2G7V5_NITMO 
ID   A0A0K2G7V5_NITMO        Unreviewed;       192 AA.
AC   A0A0K2G7V5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Sulfopyruvate decarboxylase, beta subunit {ECO:0000313|EMBL:ALA57038.1};
DE            EC=4.1.1.79 {ECO:0000313|EMBL:ALA57038.1};
GN   Name=comE {ECO:0000313|EMBL:ALA57038.1};
GN   ORFNames=NITMOv2_0602 {ECO:0000313|EMBL:ALA57038.1};
OS   Nitrospira moscoviensis.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA57038.1, ECO:0000313|Proteomes:UP000069205};
RN   [1] {ECO:0000313|EMBL:ALA57038.1, ECO:0000313|Proteomes:UP000069205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA57038.1,
RC   ECO:0000313|Proteomes:UP000069205};
RX   PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA   Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA   Nielsen P.H., Wagner M., Daims H.;
RT   "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT   from the genus Nitrospira.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011801; ALA57038.1; -; Genomic_DNA.
DR   RefSeq; WP_053378441.1; NZ_CP011801.1.
DR   AlphaFoldDB; A0A0K2G7V5; -.
DR   STRING; 42253.NITMOv2_0602; -.
DR   KEGG; nmv:NITMOv2_0602; -.
DR   PATRIC; fig|42253.5.peg.596; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000069205; Chromosome.
DR   GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
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   Lyase {ECO:0000313|EMBL:ALA57038.1};
KW   Pyruvate {ECO:0000313|EMBL:ALA57038.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069205}.
FT   DOMAIN          45..162
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   192 AA;  21036 MW;  99DBF1E89F8EA14A CRC64;
     MRPEQGTLIS RAQAMAALLE LITDQPLIVC NGFPSREVQK IADRPQNFYM IGSMGNAPAI
     ALGVALAKPT KQVITFDGDG NVLMGMGTLA TVGALKPRNF IHVVFDNEVY GTTGNQPTIS
     NVVPLEKVAK AAGYVNVERV LDREDLVYEF KDMLKKDGPS MLLIKVNEFT EEAERIVLDP
     PDVAKRFMDA IK
//
DBGET integrated database retrieval system