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