MOEZ_MYCTU
ID MOEZ_MYCTU Reviewed; 392 AA.
AC P9WMN7; 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 48.
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=Rv3206c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12123450; DOI=10.1046/j.1365-2958.2002.03005.x;
RA Manganelli R., Voskuil M.I., Schoolnik G.K., Dubnau E., Gomez M., Smith I.;
RT "Role of the extracytoplasmic-function sigma factor sigma(H) in
RT Mycobacterium tuberculosis global gene expression.";
RL Mol. Microbiol. 45:365-374(2002).
RN [3]
RP FUNCTION IN CYSO-THIOCARBOXYLATE BIOSYNTHESIS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16104727; DOI=10.1021/ja053476x;
RA Burns K.E., Baumgart S., Dorrestein P.C., Zhai H., McLafferty F.W.,
RA Begley T.P.;
RT "Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium
RT tuberculosis.";
RL J. Am. Chem. Soc. 127:11602-11603(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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) (Probable). The sulfur source is unknown.
CC {ECO:0000269|PubMed:16104727, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated under oxidative stress conditions.
CC {ECO:0000269|PubMed:12123450}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46021.1; -; Genomic_DNA.
DR PIR; G70594; G70594.
DR RefSeq; WP_003416855.1; NZ_NVQJ01000003.1.
DR RefSeq; YP_177942.1; NC_000962.3.
DR AlphaFoldDB; P9WMN7; -.
DR SMR; P9WMN7; -.
DR STRING; 83332.Rv3206c; -.
DR PaxDb; P9WMN7; -.
DR DNASU; 888871; -.
DR GeneID; 888871; -.
DR KEGG; mtu:Rv3206c; -.
DR TubercuList; Rv3206c; -.
DR eggNOG; COG0476; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR OMA; MIYDALE; -.
DR PhylomeDB; P9WMN7; -.
DR BioCyc; MetaCyc:G185E-7476-MON; -.
DR Reactome; R-MTU-936654; Cysteine synthesis from O-phosphoserine.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MTBBASE.
DR GO; GO:0016782; F:transferase activity, transferring sulphur-containing groups; TAS:Reactome.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IDA:MTBBASE.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; TAS:Reactome.
DR GO; GO:0042783; P:evasion of host immune response; IMP:MTBBASE.
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 1: Evidence at protein level;
KW ATP-binding; Membrane; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..392
FT /note="Probable adenylyltransferase/sulfurtransferase MoeZ"
FT /id="PRO_0000401136"
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
