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Database: UniProt
Entry: D1BSZ7_XYLCX
LinkDB: D1BSZ7_XYLCX
Original site: D1BSZ7_XYLCX 
ID   D1BSZ7_XYLCX            Unreviewed;       432 AA.
AC   D1BSZ7;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Xcel_1819 {ECO:0000313|EMBL:ACZ30839.1};
OS   Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 /
OS   XIL07).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Xylanimonas.
OX   NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ30839.1, ECO:0000313|Proteomes:UP000002255};
RN   [1] {ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Foster B., Clum A., 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., Gehrich-Schroeter G., Schneider S., Pukall S.R.,
RA   Klenk H.P., Eisen J.A.;
RT   "The complete chromosome of Xylanimonas cellulosilytica DSM 15894.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ30839.1, ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RX   PubMed=21304672; DOI=10.4056/sigs.571102;
RA   Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F.,
RA   Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K.,
RA   Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Xylanimonas cellulosilytica type strain
RT   (XIL07).";
RL   Stand. Genomic Sci. 2:1-8(2010).
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; CP001821; ACZ30839.1; -; Genomic_DNA.
DR   RefSeq; WP_012878581.1; NC_013530.1.
DR   AlphaFoldDB; D1BSZ7; -.
DR   STRING; 446471.Xcel_1819; -.
DR   KEGG; xce:Xcel_1819; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_11; -.
DR   OMA; PRFDNSQ; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002255; 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   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:UP000002255};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          205..350
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   432 AA;  43061 MW;  B2C4D56ACCABF9B0 CRC64;
     MSRTSPAEHA ARVARLLAPA LAGRRTERVL VADLLAAARQ AAVLPPRVLA RDARAIVALP
     GFDNSQMDGF AVRAADLTAA TPAAPVRLPV GPAVPAGTAP APLAPGTAAP VMTGAPIPPG
     ADAVVRIEDA DPPGFGAGPG GGVTVTSAAF ARPVAAGTYV RTAGSDVSAS AVVVAAETTL
     GPAQLGALVA AGVADVEVWA PPHVLLLSTG SELVPAGRPL GPAQVFDANG AALTAALAQV
     GCRVTARVVP DDPAALLSAL HETQDADLVL TTGGVSAGAY EVVRSTLDDA WFGPVAMQPG
     GPQGLGTVAV RPAGNGDADP ARIVPLVAFP GNPVSALVSF ELFLRPVLAR ATGTVPATRP
     ARRAPLAEPV DSPPALLQVR RGRLDDDGRV RLVGGPGSHL LAHLAAATVL VHVPPGVARL
     EAGTAVDIWE IS
//
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