ID   MOAE_HALVD              Reviewed;         261 AA.
AC   D4GSW7;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Probable molybdopterin synthase;
DE            Short=MPT synthase;
DE            EC=2.8.1.-;
GN   Name=moaE; OrderedLocusNames=HVO_1864; ORFNames=C498_04590;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [3]
RP   SAMPYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20054389; DOI=10.1038/nature08659;
RA   Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., Zhou G.,
RA   Chen S., Wells L., Maupin-Furlow J.A.;
RT   "Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax
RT   volcanii.";
RL   Nature 463:54-60(2010).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DS2 / DS70;
RX   PubMed=21368171; DOI=10.1073/pnas.1018151108;
RA   Miranda H.V., Nembhard N., Su D., Hepowit N., Krause D.J., Pritz J.R.,
RA   Phillips C., Soll D., Maupin-Furlow J.A.;
RT   "E1- and ubiquitin-like proteins provide a direct link between protein
RT   conjugation and sulfur transfer in archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4417-4422(2011).
RN   [5]
RP   SAMPYLATION AT LYS-240 AND LYS-247 WITH SAMP1.
RC   STRAIN=DS2 / DS70;
RX   PubMed=22970855; DOI=10.1111/mmi.12038;
RA   Hepowit N.L., Uthandi S., Miranda H.V., Toniutti M., Prunetti L.,
RA   Olivarez O., De Vera I.M., Fanucci G.E., Chen S., Maupin-Furlow J.A.;
RT   "Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-like
RT   small archaeal modifier proteins (SAMPs) from protein-conjugates.";
RL   Mol. Microbiol. 86:971-987(2012).
RN   [6]
RP   SAMPYLATION AT LYS-240 AND LYS-247 WITH SAMP3.
RC   STRAIN=DS2 / DS70;
RX   PubMed=24097257; DOI=10.1074/mcp.m113.029652;
RA   Miranda H.V., Antelmann H., Hepowit N., Chavarria N.E., Krause D.J.,
RA   Pritz J.R., Basell K., Becher D., Humbard M.A., Brocchieri L.,
RA   Maupin-Furlow J.A.;
RT   "Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-
RT   dependent mechanism.";
RL   Mol. Cell. Proteomics 13:220-239(2014).
CC   -!- FUNCTION: Converts molybdopterin precursor Z into molybdopterin. This
CC       requires the incorporation of two sulfur atoms into precursor Z to
CC       generate a dithiolene group. The sulfur is provided by the
CC       thiocarboxylated form of SAMP1 (Probable).
CC       {ECO:0000305|PubMed:21368171}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- PTM: Sampylated at Lys-240 and Lys-247 with the archaeal ubiquitin-like
CC       proteins SAMP1 and SAMP3, which may regulate enzymatic activity.
CC       {ECO:0000269|PubMed:20054389, ECO:0000269|PubMed:22970855,
CC       ECO:0000269|PubMed:24097257}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow anaerobically
CC       with DMSO and do not show DMSO reductase activity although dmsA
CC       transcript is present, indicating lack of maturation of the DmsA
CC       apoprotein into the MoCo-holoprotein. Their growth in the presence of
CC       oxygen is not affected. Disruption of this gene does not affect the
CC       formation of SAMP-protein conjugates. {ECO:0000269|PubMed:21368171}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MoaE family.
CC       {ECO:0000305}.
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DR   EMBL; CP001956; ADE02555.1; -; Genomic_DNA.
DR   EMBL; AOHU01000036; ELY34758.1; -; Genomic_DNA.
DR   RefSeq; WP_004041746.1; NZ_AOHU01000036.1.
DR   AlphaFoldDB; D4GSW7; -.
DR   SMR; D4GSW7; -.
DR   STRING; 309800.C498_04590; -.
DR   EnsemblBacteria; ADE02555; ADE02555; HVO_1864.
DR   EnsemblBacteria; ELY34758; ELY34758; C498_04590.
DR   GeneID; 8925765; -.
DR   KEGG; hvo:HVO_1864; -.
DR   PATRIC; fig|309800.29.peg.892; -.
DR   eggNOG; arCOG00533; Archaea.
DR   HOGENOM; CLU_088141_0_0_2; -.
DR   OMA; EFWVHDR; -.
DR   OrthoDB; 62565at2157; -.
DR   BioCyc; MetaCyc:MON-20242; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000008243; Chromosome.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00756; MoaE; 1.
DR   Gene3D; 3.90.1170.40; -; 1.
DR   InterPro; IPR036563; MoaE_sf.
DR   InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR   Pfam; PF02391; MoaE; 1.
DR   SUPFAM; SSF54690; SSF54690; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Molybdenum cofactor biosynthesis; Reference proteome;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..261
FT                   /note="Probable molybdopterin synthase"
FT                   /id="PRO_0000428941"
FT   BINDING         156..158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP1); alternate"
FT   CROSSLNK        240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP3); alternate"
FT   CROSSLNK        247
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP1); alternate"
FT   CROSSLNK        247
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP3); alternate"
SQ   SEQUENCE   261 AA;  27935 MW;  5143F3D6DEA80D92 CRC64;
     MHVLGIVGAG ATTLCDRLAA QLDGRVATVE SLPESATEPE STDGVAAAYG LSPDGNWVGS
     GDDRDLDGLL DDLSAEYDYA LLSGFPDARV PTVALAGVDA ANVVAEAETA DAADVASLAA
     EIDSHEPHVT LETLVERAKA DPLEVYAGAI ATFTGRVRAK ESEDDDPTLS LEFEKYDGVA
     ESKMDAISEE LEARDGVLRV LMHHRVGVVE DGADIVFVVV LAGHRREAFR TVEDGIDRLK
     DEVPIFKKET TTDEEFWVHD R