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Database: UniProt
Entry: I2B3V1_SHIBC
LinkDB: I2B3V1_SHIBC
Original site: I2B3V1_SHIBC 
ID   I2B3V1_SHIBC            Unreviewed;       195 AA.
AC   I2B3V1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=N-terminal part of formate dehydrogenase-O {ECO:0000313|EMBL:AFJ45205.1};
GN   OrderedLocusNames=EBL_c00690 {ECO:0000313|EMBL:AFJ45205.1};
OS   Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS   CDC 9005-74) (Escherichia blattae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shimwellia.
OX   NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ45205.1, ECO:0000313|Proteomes:UP000001955};
RN   [1] {ECO:0000313|EMBL:AFJ45205.1, ECO:0000313|Proteomes:UP000001955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC   {ECO:0000313|Proteomes:UP000001955};
RX   PubMed=22843577; DOI=10.1128/JB.00829-12;
RA   Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT   "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT   DSM 4481, isolated from a cockroach.";
RL   J. Bacteriol. 194:4436-4436(2012).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP001560; AFJ45205.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2B3V1; -.
DR   STRING; 630626.EBL_c00690; -.
DR   KEGG; ebt:EBL_c00690; -.
DR   PATRIC; fig|630626.3.peg.71; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_061371_1_1_6; -.
DR   Proteomes; UP000001955; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43598:SF6; FORMATE DEHYDROGENASE-O MAJOR SUBUNIT; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001955}.
FT   DOMAIN          43..106
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   195 AA;  21267 MW;  CF7F2A6E1970DC8C CRC64;
     MQVSRRQFFK ICAGGMAGTT AAALGFTPAT ALAETRQYKL LRTRETRNTC TYCSVGCGLL
     MYSLGDGAKN AKASIFHIEG DPDHPVNRGA LCPKGAGLVD FIHSESRLKT PQYRAPGSDK
     WQDISWDDAF DRIAKLMKAD RDANFIAQND QGTTVNRWLS TGMLCASASS NETGYLTQKF
     SRALGMLAVD NQARV
//
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