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Database: UniProt
Entry: D1B4Z2_SULD5
LinkDB: D1B4Z2_SULD5
Original site: D1B4Z2_SULD5 
ID   D1B4Z2_SULD5            Unreviewed;       404 AA.
AC   D1B4Z2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Sdel_2150 {ECO:0000313|EMBL:ACZ13162.1};
OS   Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurospirillaceae; Sulfurospirillum.
OX   NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ13162.1, ECO:0000313|Proteomes:UP000002222};
RN   [1] {ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
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   Ovchinnikova G., Munk A.C., Lu M., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Aumann P., Schneider S., Lang E.,
RA   Spring S., Klenk H.P., Eisen J.A.;
RT   "The complete genome of Sulfurospirillum deleyianum DSM 6946.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ13162.1, ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
RX   PubMed=21304697; DOI=10.4056/sigs.671209;
RA   Sikorski J., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., Goodwin L.,
RA   Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Detter J.C., Han C., Rohde M., Lang E., Spring S., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Sulfurospirillum deleyianum type strain
RT   (5175).";
RL   Stand. Genomic Sci. 2:149-157(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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP001816; ACZ13162.1; -; Genomic_DNA.
DR   RefSeq; WP_012857907.1; NC_013512.1.
DR   AlphaFoldDB; D1B4Z2; -.
DR   STRING; 525898.Sdel_2150; -.
DR   KEGG; sdl:Sdel_2150; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_7; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002222; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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   Membrane {ECO:0000256|SAM:Phobius};
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:UP000002222};
KW   Transferase {ECO:0000256|RuleBase:RU365090};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        292..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          178..317
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   404 AA;  44678 MW;  35AE73F5C1D4B3EC CRC64;
     MSQNFPPFDE TLRALEASIC TQFGVENLFV GEALGRFLAV DIVAVENNPT HETASMDGYA
     IAFSDQDLGK LHVNAFVPAG SETTGVVAQG QCVKTFTGTL MSEGTDTLIP IENVEVEGES
     IRITTPVFKG HAVRPVGENY KAGEVLIQKG TKIGFAEIGV MAELGMVQVE VFMRPRIAIL
     STGNEILDFG EVKTSHAQIR SSNHVTVEAI LRQMGCETMR FKLIRDERDV IEQQLRQALM
     WSDIVVTTGG GSVGDFDYLQ SILTDMKIQN IIDGSYMKPG RHIRVVKTGH KYIYALPGFP
     YSASVCTFLF IAPLFRKMRS QKFALPTIKA KMGEFYKKRS KFVEFTACNL RFCEGELVVD
     LKGKKEGSSA ILNNLLDKPS LLRVEKDVLK IEKGEMVDVV LLDV
//
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