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Database: UniProt
Entry: Q0AYS0_SYNWW
LinkDB: Q0AYS0_SYNWW
Original site: Q0AYS0_SYNWW 
ID   Q0AYS0_SYNWW            Unreviewed;       236 AA.
AC   Q0AYS0;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0000259|Pfam:PF00899};
GN   OrderedLocusNames=Swol_0813 {ECO:0000313|EMBL:ABI68134.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI68134.1, ECO:0000313|Proteomes:UP000001968};
RN   [1] {ECO:0000313|Proteomes:UP000001968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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DR   EMBL; CP000448; ABI68134.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0AYS0; -.
DR   STRING; 335541.Swol_0813; -.
DR   KEGG; swo:Swol_0813; -.
DR   eggNOG; COG1179; Bacteria.
DR   HOGENOM; CLU_013325_4_1_9; -.
DR   OMA; DMDDICV; -.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd00755; YgdL_like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        208..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..231
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   236 AA;  26015 MW;  4E314B0E1C9B7CED CRC64;
     MMSDRIFQRT ELLIGQEAME TLRVSCMLVI GLGGVGSYAA EAIARCGVGR IILCDPDRVE
     ASNINRQLVA LNSTRGELKT EVMSQRLRDI NPGLQLKEYP FSYTGESSAE ILSEEIHFVL
     DAIDSLPDKI HLIKTCLHRK IPVISSMGTA NRLDPLLLTI ADIKDSIICP VARKLRRELR
     RENIFQGVPV VYSRETPVKT AYSGETRLGS ISFVPAVAGL LLASYAVKQL ISMNNG
//
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