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MOEZ_MYCTO
ID   MOEZ_MYCTO              Reviewed;         392 AA.
AC   P9WMN6; L0TDG4; Q6MWZ9; Q7D5X9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable adenylyltransferase/sulfurtransferase MoeZ;
DE   Includes:
DE     RecName: Full=Sulfur carrier protein CysO adenylyltransferase;
DE              EC=2.7.7.-;
DE   Includes:
DE     RecName: Full=Sulfur carrier protein CysO sulfurtransferase;
DE              EC=2.8.1.-;
GN   Name=moeZ; Synonyms=moeB1; OrderedLocusNames=MT3301;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the conversion of the sulfur carrier protein CysO
CC       to CysO-thiocarboxylate. The reaction is thought to proceed in two
CC       steps: first, ATP-dependent activation of CysO as acyl-adenylate (CysO-
CC       COOAMP), followed by sulfur transfer to give CysO-thiocarboxylate
CC       (CysO-COSH) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47644.1; -; Genomic_DNA.
DR   PIR; G70594; G70594.
DR   RefSeq; WP_003416855.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMN6; -.
DR   SMR; P9WMN6; -.
DR   EnsemblBacteria; AAK47644; AAK47644; MT3301.
DR   KEGG; mtc:MT3301; -.
DR   PATRIC; fig|83331.31.peg.3554; -.
DR   HOGENOM; CLU_013325_1_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.250.10; -; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Membrane; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..392
FT                   /note="Probable adenylyltransferase/sulfurtransferase MoeZ"
FT                   /id="PRO_0000427272"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          300..390
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        203
FT                   /note="Glycyl thioester intermediate; for
FT                   adenylyltransferase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        350
FT                   /note="Cysteine persulfide intermediate; for
FT                   sulfurtransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  42173 MW;  06970A1BD2CC9645 CRC64;
     MSTSLPPLVE PASALSREEV ARYSRHLIIP DLGVDGQKRL KNARVLVIGA GGLGAPTLLY
     LAAAGVGTIG IVDFDVVDES NLQRQVIHGV ADVGRSKAQS ARDSIVAINP LIRVRLHELR
     LAPSNAVDLF KQYDLILDGT DNFATRYLVN DAAVLAGKPY VWGSIYRFEG QASVFWEDAP
     DGLGVNYRDL YPEPPPPGMV PSCAEGGVLG IICASVASVM GTEAIKLITG IGETLLGRLL
     VYDALEMSYR TITIRKDPST PKITELVDYE QFCGVVADDA AQAAKGSTIT PRELRDWLDS
     GRKLALIDVR DPVEWDIVHI DGAQLIPKSL INSGEGLAKL PQDRTAVLYC KTGVRSAEAL
     AAVKKAGFSD AVHLQGGIVA WAKQMQPDMV MY
 
 
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