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Database: UniProt
Entry: B6BHQ9_SULGG
LinkDB: B6BHQ9_SULGG
Original site: B6BHQ9_SULGG 
ID   B6BHQ9_SULGG            Unreviewed;       318 AA.
AC   B6BHQ9; H1FTU4;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=PorB {ECO:0000313|EMBL:EHP30058.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:EHP30058.1};
GN   Name=porB {ECO:0000313|EMBL:EHP30058.1};
GN   ORFNames=SMGD1_1534 {ECO:0000313|EMBL:EHP30058.1};
OS   Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP30058.1, ECO:0000313|Proteomes:UP000006431};
RN   [1] {ECO:0000313|EMBL:EHP30058.1, ECO:0000313|Proteomes:UP000006431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD1 {ECO:0000313|EMBL:EHP30058.1,
RC   ECO:0000313|Proteomes:UP000006431};
RX   PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA   Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA   Labrenz M., Jurgens K.;
RT   "Genome and physiology of a model Epsilonproteobacterium responsible for
RT   sulfide detoxification in marine oxygen depletion zones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
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:EHP30058.1}.
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DR   EMBL; AFRZ01000001; EHP30058.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6BHQ9; -.
DR   SMR; B6BHQ9; -.
DR   STRING; 929558.SMGD1_1534; -.
DR   PATRIC; fig|929558.5.peg.1525; -.
DR   eggNOG; COG1013; Bacteria.
DR   HOGENOM; CLU_058423_0_0_7; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000006431; Unassembled WGS sequence.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03376; TPP_PFOR_porB_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EHP30058.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006431}.
FT   DOMAIN          53..222
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          151..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  35665 MW;  60FA786CDFC0FC9A CRC64;
     MSEMKKIKNL KEFSTSADRF EGANLLCPGC AHSIIVREVL NATNDDLVLS ASTGCLEVCT
     AVYPYTSWDA SWIHIGFENG STAVAGAEAM YKALKNKGRL KQPDRNPKFV SFAGDGASYD
     IGFQWISGCM ERGHNMMHVV LDNEVYANTG GQRSSSTPIG SSTTTAPAGR VSYGEKKNKK
     DMVSIMASHH IPYSAQVSPN KWKDMVKKIQ HGFSVDGPVF INAVSPCTTE WKFDPKDTML
     LADLSTDSLV FPLYEIIDGR ELNITYRPKN VVPVEEYLAA QGRFKHLFKD EYKHLIKEWQ
     DRVDDNWSYL QRREEARV
//
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