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MOAD_HAEIN
ID   MOAD_HAEIN              Reviewed;          81 AA.
AC   P45309;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Molybdopterin synthase sulfur carrier subunit;
DE   AltName: Full=MPT synthase subunit 1;
DE   AltName: Full=Molybdenum cofactor biosynthesis protein D;
DE   AltName: Full=Molybdopterin-converting factor small subunit;
DE   AltName: Full=Molybdopterin-converting factor subunit 1;
DE   AltName: Full=Sulfur carrier protein MoaD;
GN   Name=moaD; OrderedLocusNames=HI_1674;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in sulfur transfer in the conversion of
CC       molybdopterin precursor Z to molybdopterin. {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Forms a
CC       stable heterotetrameric complex of 2 MoaD and 2 MoeB during adenylation
CC       of MoaD by MoeB. During catalysis MoaD shuttles between the two
CC       heterotetrameric complexes (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MoaD family. {ECO:0000305}.
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DR   EMBL; L42023; AAC23319.1; -; Genomic_DNA.
DR   PIR; A59368; A59368.
DR   RefSeq; NP_439816.1; NC_000907.1.
DR   RefSeq; WP_005654167.1; NC_000907.1.
DR   AlphaFoldDB; P45309; -.
DR   SMR; P45309; -.
DR   STRING; 71421.HI_1674; -.
DR   EnsemblBacteria; AAC23319; AAC23319; HI_1674.
DR   KEGG; hin:HI_1674; -.
DR   PATRIC; fig|71421.8.peg.1753; -.
DR   eggNOG; COG1977; Bacteria.
DR   HOGENOM; CLU_114601_4_0_6; -.
DR   OMA; DRVHAKP; -.
DR   PhylomeDB; P45309; -.
DR   BioCyc; HINF71421:G1GJ1-1689-MON; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR044672; MOCS2A.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR003749; ThiS/MoaD-like.
DR   PANTHER; PTHR33359; PTHR33359; 1.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; SSF54285; 1.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..81
FT                   /note="Molybdopterin synthase sulfur carrier subunit"
FT                   /id="PRO_0000209132"
FT   MOD_RES         81
FT                   /note="1-thioglycine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         81
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   81 AA;  8826 MW;  35D1440F82456F22 CRC64;
     MLNVLFFAQT RELIGVDAIQ LEDDFATAEA VREHLAQKGD KWALALEKGK LLVAINQTLM
     PLESAVKNGD EIAFFPPVTG G
 
 
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