ID   A0A0P7XH01_9RHOB        Unreviewed;       351 AA.
AC   A0A0P7XH01;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Dinucleotide-utilizing enzymes involved in molybdopterin and thiamine biosynthesis family 2 {ECO:0000313|EMBL:KPQ15494.1};
GN   ORFNames=HLUCCO18_11785 {ECO:0000313|EMBL:KPQ15494.1};
OS   Rhodobacteraceae bacterium HLUCCO18.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ15494.1, ECO:0000313|Proteomes:UP000050333};
RN   [1] {ECO:0000313|EMBL:KPQ15494.1, ECO:0000313|Proteomes:UP000050333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ15494.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) 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:KPQ15494.1}.
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DR   EMBL; LJSY01000027; KPQ15494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7XH01; -.
DR   STRING; 1666917.HLUCCO18_11785; -.
DR   PATRIC; fig|1666917.4.peg.1128; -.
DR   Proteomes; UP000050333; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          111..347
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   351 AA;  36560 MW;  DE0CD4A2698D063F CRC64;
     MLLVALLAAV IWGIGAAMGV PRAARVNMLG LLFVIVLALQ IVLPDGHPVR EATGGSPALW
     LILAAGVVLV LLYRAILNRL RGQAAEIEAT RESVEPAISD GPFSDAELER YARHITLPDI
     GGGGQLALKN AKVLVIGAGG LGAPALLYLA AAGVGRIGIV DGDTVALSNL QRQVIHTDAR
     QDMPKVFSAQ AAIEALNPHV DTRPYNRALT ADIAEELFAE YDLILDGTDS YETRALVNRA
     AVAVGRPVLA GAISAWEGQI TLYDPASGAP CMACVFPRAP EPGLAATCAE TGVIGALPGV
     VGSMMALEAV KHITGAGRGL SGRMLIYDGL HAEMRSFAMK RRPDCPVCGS I
//