ID   F2GAN0_ALTMD            Unreviewed;       253 AA.
AC   F2GAN0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Molybdopterin biosynthesis protein MoeB {ECO:0000313|EMBL:AEA99994.1};
GN   OrderedLocusNames=MADE_1019360 {ECO:0000313|EMBL:AEA99994.1};
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373 {ECO:0000313|EMBL:AEA99994.1, ECO:0000313|Proteomes:UP000001870};
RN   [1] {ECO:0000313|EMBL:AEA99994.1, ECO:0000313|Proteomes:UP000001870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype
RC   {ECO:0000313|Proteomes:UP000001870};
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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DR   EMBL; CP001103; AEA99994.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2GAN0; -.
DR   KEGG; amc:MADE_1019360; -.
DR   HOGENOM; CLU_013325_10_3_6; -.
DR   Proteomes; UP000001870; Chromosome.
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:SF194; MOLYBDOPTERIN-SYNTHASE ADENYLYLTRANSFERASE; 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;
FT   DOMAIN          12..246
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   253 AA;  27888 MW;  E01B4F36CFC69F04 CRC64;
     MKDLTTEQAM RYSRHILLSD FDLERQEALV NCSVLVIGVG GLGCAASQYL TASGVGHLTL
     VDDDKVELTN LQRQVLHTEK SVGANKVDSA QLALQQINSE VNITTLCLRP SEKQLDELIA
     KQDVVLDCTD NLESRNRINQ ICYRQSIPLV SGAAIRMEGQ ILCIDPRQQS ACYACVSHFF
     GEQNLSCVES GVMSPLVGII GAMQALEAIK LVTHYGKPLC NRLHLYDAMQ ATWSEFKVTR
     QQDCQVCGSK AKL
//