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Database: UniProt
Entry: L0K8Z6_HALHC
LinkDB: L0K8Z6_HALHC
Original site: L0K8Z6_HALHC 
ID   L0K8Z6_HALHC            Unreviewed;       341 AA.
AC   L0K8Z6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Halha_1060 {ECO:0000313|EMBL:AGB41020.1};
OS   Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Halobacteroides.
OX   NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB41020.1, ECO:0000313|Proteomes:UP000010880};
RN   [1] {ECO:0000313|Proteomes:UP000010880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC   {ECO:0000313|Proteomes:UP000010880};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Halobacteroides halobius DSM 5150.";
RL   Submitted (FEB-2012) 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|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;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP003359; AGB41020.1; -; Genomic_DNA.
DR   RefSeq; WP_015326745.1; NC_019978.1.
DR   AlphaFoldDB; L0K8Z6; -.
DR   STRING; 748449.Halha_1060; -.
DR   KEGG; hhl:Halha_1060; -.
DR   PATRIC; fig|748449.3.peg.1015; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_068847_1_0_9; -.
DR   OMA; LNGADWV; -.
DR   OrthoDB; 9767940at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000010880; 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; cd03522; MoeA_like; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF28; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 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:UP000010880};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          175..307
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   341 AA;  37904 MW;  A1C7D4356EAF09CE CRC64;
     MGIKKIPVEE AVGRVVAHDM TQIVPEKFKG ARFKKGDLID NSDISTLKDM GKEHIYVLTL
     EEGIIHEDDA AYRIAKHVIG KNIALSEVNE GKITLKAQQK GILKVEKDLL LKVNSSNQIL
     ITSSHNNMFL QAGDSIAGVR INPLTIEEEK LEKVEDIIRD QSIFKIEPIV NKKVGIVVTG
     SEVYNGRIKD QFVPTLQKKF QRWGGELLNS IIVPDEVDQI TAALSSLKES GAEILITGGG
     MSVDPDDLTP QGIRNTGAQI IKYGIPVLPG NKLMLAYWDD IPILGLPACV IFEKITVFDL
     VYPRLLTEEH ITRNDLIELS YGGYCHHCEI CQFPKCSFGR F
//
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