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Database: UniProt
Entry: L5M408_MYODS
LinkDB: L5M408_MYODS
Original site: L5M408_MYODS 
ID   L5M408_MYODS            Unreviewed;       613 AA.
AC   L5M408;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Gephyrin {ECO:0000256|RuleBase:RU365090};
DE   Includes:
DE     RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE              Short=MPT Mo-transferase {ECO:0000256|RuleBase:RU365090};
DE              EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
DE     AltName: Full=Domain E {ECO:0000256|RuleBase:RU365090};
DE   Includes:
DE     RecName: Full=Molybdopterin adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE              Short=MPT adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE              EC=2.7.7.75 {ECO:0000256|RuleBase:RU365090};
DE     AltName: Full=Domain G {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=MDA_GLEAN10010915 {ECO:0000313|EMBL:ELK32980.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK32980.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC       cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC       molybdate is inserted into adenylated molybdopterin and AMP is
CC       released. {ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC         diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC         ChEBI:CHEBI:62727; Evidence={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}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC       {ECO:0000256|ARBA:ARBA00008339}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC       {ECO:0000256|ARBA:ARBA00007589}.
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DR   EMBL; KB104801; ELK32980.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5M408; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; 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   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
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; 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   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 2.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 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:UP000010556};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          62..172
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|Pfam:PF00994"
FT   DOMAIN          388..552
FT                   /note="MoeA N-terminal and linker"
FT                   /evidence="ECO:0000259|Pfam:PF03453"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  65795 MW;  ADB5FB849BE62946 CRC64;
     MPSAGASGTG TVSTWEWWQR ERGCRQTGDQ GPLWEEPSGG TENGPRPTPV PTADSQPTVP
     FEETLIDWCD EKELNLILTT GGTGFAPRDV TPEKFPTFPF CGLQKGATKE VIEREAPGMA
     LAMLMGSLNV TPLGMLSRPV CGIRGKTLII NLPGSKKGSQ ECFQFILPAL PHAIDLLRDA
     IVKVKEVHDE LEDLPSPPPP LSPPPTTSPH KQTEDKGVQC EEEEEEKKDS GVASTEDSSS
     SHITAAAIAA KKHPFYTSPA VIMAHGEQPI PGLISYSHHA TGSADERIPD SIISRGVQVL
     PRDTASLSTT PSESPRAQAT SRLSTASCPT PKQIRRPDES KGVASRVGSL KVQSRCSSKE
     NILRASHSAV DITKVARRHR MSPFPLTSMD KAFITVLEMT PVLGTEIINY RDGMGRVLAQ
     DVYAKDNLPP FPASVKDGYA VRAADGPGDR FIIGESQAGE QPTQTVMPGQ VMRVTTGAPI
     PCGADAVVQV EDTELIRESD DGTEELEVRI LVQARPGQDI RPIGHDIKRG ECVLAKGTHM
     GPSEIGLLAT VGVTEVEVNK FPVVAVMSTG NELLNPEDDL LPGKIRDSNR STLLATIQEH
     GYPTINLGIV GDK
//
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