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Database: UniProt
Entry: F2LY95_HIPMA
LinkDB: F2LY95_HIPMA
Original site: F2LY95_HIPMA 
ID   F2LY95_HIPMA            Unreviewed;       390 AA.
AC   F2LY95;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Hipma_1462 {ECO:0000313|EMBL:AEA34418.1};
OS   Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2).
OC   Bacteria; Campylobacterota; Desulfurellia; Desulfurellales; Hippeaceae;
OC   Hippea.
OX   NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA34418.1, ECO:0000313|Proteomes:UP000008139};
RN   [1] {ECO:0000313|EMBL:AEA34418.1, ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RX   PubMed=21886857;
RA   Huntemann M., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Rohde M., Spring S., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Mavromatis K.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer Hippea
RT   maritima type strain (MH(2)).";
RL   Stand. Genomic Sci. 4:303-311(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Hippea maritima DSM 10411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP.
CC       {ECO:0000256|ARBA:ARBA00002901, ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC         molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC         ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001529};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP002606; AEA34418.1; -; Genomic_DNA.
DR   RefSeq; WP_013682447.1; NC_015318.1.
DR   AlphaFoldDB; F2LY95; -.
DR   STRING; 760142.Hipma_1462; -.
DR   KEGG; hmr:Hipma_1462; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_7; -.
DR   InParanoid; F2LY95; -.
DR   OMA; KMPKVAF; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000008139; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR036135; MoeA_linker/N_sf.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008139};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          166..304
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   390 AA;  43720 MW;  231330535A22B87F CRC64;
     MLRVDDAIDV ILSNVFPIDG WDEVFLDNAL NRVAFEDVVS NIDVPDFDRS AMDGYALVFG
     DDKKRFRVVE SADELEENCC IRINTGFPIP DKADAIAEVE ITKRVGNYIE LLKPVERKRN
     FTSKGIELKK GGLLLKKGER ISVRKQALLA YSGVFKLKVF RVPIVGIITT GDEVIFAGDE
     FESGKVYNAN YFILKGLVQK WLGSPVYFGH IKDDKALLKK TIRHTLKRCD ILLTTGGVSM
     GSRDFIKSVL SDMDANIFFE KTTIKPGKPA VFAKIEDKPF FGLPGWPAAL FTVAYVYLKP
     MLFKLAGIDK LANEYLNCII DESMHSKMGK CYFDRVRLTI TDGMYHGVSA GSQKTDNFYS
     VAVADGLVRI DEKEEDKEKG AELPLIVFDD
//
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