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Database: UniProt
Entry: A0A164A8L8_9BACI
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ID   A0A164A8L8_9BACI        Unreviewed;       337 AA.
AC   A0A164A8L8; A0A165Y7E3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   03-MAY-2023, entry version 19.
DE   SubName: Full=Thiamine biosynthesis protein MoeB {ECO:0000313|EMBL:KZN96801.1};
GN   ORFNames=AZI98_06670 {ECO:0000313|EMBL:KZN96801.1};
OS   Aeribacillus pallidus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aeribacillus.
OX   NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN96801.1, ECO:0000313|Proteomes:UP000076476};
RN   [1] {ECO:0000313|EMBL:KZN96801.1, ECO:0000313|Proteomes:UP000076476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8m3 {ECO:0000313|EMBL:KZN96801.1,
RC   ECO:0000313|Proteomes:UP000076476};
RA   Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M., Korshunova A.V.,
RA   Sokolova D.S.;
RT   "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum
RT   reservoir.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZN96801.1}.
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DR   EMBL; LWBR01000014; KZN96801.1; -; Genomic_DNA.
DR   RefSeq; WP_063387505.1; NZ_SFCD01000026.1.
DR   AlphaFoldDB; A0A164A8L8; -.
DR   STRING; 33936.AZI98_06670; -.
DR   OrthoDB; 9804286at2; -.
DR   Proteomes; UP000076476; Unassembled WGS sequence.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd00757; ThiF_MoeB_HesA_family; 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; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076476}.
FT   DOMAIN          5..238
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   337 AA;  37582 MW;  B8C132F8D741796F CRC64;
     MMERYSRQIL FSPIGEEGQK KLLKSHVLIV GAGALGCASA EMLARAGIGK ITIIDRDYVD
     WSNLGRQQLY TEEDAKQKLP KAVAAKKHLQ EINSNISIEA IVGDFSIDFI EHVKDVDLII
     DGTDNFETRF FINDLAMKHE IPWIYGAVVR SYGMTVSIVP KQTPCLHCML QAIPSDGMTC
     DTVGVISPAV QIVASYQTAE ALKYLVSGEV SKKLVSFDVW TREHSAVDMT KLKKADCPSC
     GHHPTYPYLS VENGLKTAVL CGRNTVQIRP QQKQKISLSE ITNRLRPIVK DLKGNAYLIS
     FQADDFRVVL FQDGRALIHG TKEEEKAKAI YQRYFGA
//
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