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Database: UniProt
Entry: A0A0B0HFK0_SOVGS
LinkDB: A0A0B0HFK0_SOVGS
Original site: A0A0B0HFK0_SOVGS 
ID   A0A0B0HFK0_SOVGS        Unreviewed;       420 AA.
AC   A0A0B0HFK0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=JV46_21730 {ECO:0000313|EMBL:KHF26246.1};
OS   Solemya velum gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF26246.1, ECO:0000313|Proteomes:UP000030856};
RN   [1] {ECO:0000313|EMBL:KHF26246.1, ECO:0000313|Proteomes:UP000030856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH {ECO:0000313|EMBL:KHF26246.1,
RC   ECO:0000313|Proteomes:UP000030856};
RX   PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA   Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA   Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA   Eisen J.A., Cavanaugh C.M.;
RT   "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT   velum: a blueprint for thriving in and out of symbiosis.";
RL   BMC Genomics 15:924-924(2014).
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}.
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:KHF26246.1}.
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DR   EMBL; JRAA01000001; KHF26246.1; -; Genomic_DNA.
DR   RefSeq; WP_052132094.1; NZ_JRAA01000001.1.
DR   AlphaFoldDB; A0A0B0HFK0; -.
DR   STRING; 2340.JV46_21730; -.
DR   PATRIC; fig|2340.3.peg.756; -.
DR   eggNOG; COG0303; Bacteria.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000030856; Unassembled WGS sequence.
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; IPR008284; MoCF_biosynth_CS.
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; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF34; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 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.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 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:UP000030856};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KHF26246.1}.
FT   DOMAIN          194..331
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   420 AA;  44859 MW;  E65CEB9812DEC492 CRC64;
     MTTSTRDLNN SCDCDNSREK LQPLESALDA LLCAAPGISD TETVPLHDAA GRILAVDLVS
     GIDVPPADNS AMDGYAIANA DYKGEPLRIS QRIPAGISPD PLEAGTAARI FTGAFIPANA
     DAVVMQENAS IGEDGSVSFC GEIRTGQNVR SRGEDITRNE TILNKGRRLL PQDIGLAASV
     GIGEVEVYRR VRVATFFTGS ELVQPGKPLE PGQIYNSNQS VLNALLSACG CELVSLGITE
     DTLEATIETF KQAASEADCI ITSGGVSVGE EDHVRAALES LGKIDFWRVA IKPGKPVVFG
     QVDDTPVIGL PGNPVSVFST FCLLARPFLL TMQQREDVMP VSHQVSAGFD WKKSGSRREF
     VRAQLQTDAQ GRQSAILYPN QGSGVLSSTS WAHGFVEVRE HKTVTTGDRV VFYPFSGLMS
//
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