ASLB_ECOLI
ID ASLB_ECOLI Reviewed; 411 AA.
AC P25550; Q2M8A5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 4.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Anaerobic sulfatase-maturating enzyme homolog AslB;
DE Short=AnSME homolog;
GN Name=aslB; Synonyms=atsB; OrderedLocusNames=b3800, JW5594;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Murphy H.R., Kalman M., Cashel M.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 391.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 116 AND 117.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP MEMBER OF THE RADICAL SAM SUPERFAMILY.
RX PubMed=11222759; DOI=10.1093/nar/29.5.1097;
RA Sofia H.J., Chen G., Hetzler B.G., Reyes-Spindola J.F., Miller N.E.;
RT "Radical SAM, a novel protein superfamily linking unresolved steps in
RT familiar biosynthetic pathways with radical mechanisms: functional
RT characterization using new analysis and information visualization
RT methods.";
RL Nucleic Acids Res. 29:1097-1106(2001).
RN [7]
RP NON-INVOLVEMENT IN SULFATASE MATURATION.
RC STRAIN=K12 / BW25113;
RX PubMed=17303125; DOI=10.1016/j.febslet.2007.01.076;
RA Benjdia A., Deho G., Rabot S., Berteau O.;
RT "First evidences for a third sulfatase maturation system in prokaryotes
RT from E. coli aslB and ydeM deletion mutants.";
RL FEBS Lett. 581:1009-1014(2007).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q0TTH1};
CC Note=Binds 3 [4Fe-4S] clusters (By similarity). The first cluster is
CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine (By similarity). {ECO:0000250|UniProtKB:Q0TTH1};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000305}.
CC -!- CAUTION: Despite its homology to the anaerobic sulfatase-maturating
CC enzymes, it is not involved in Cys-type sulfatase maturation in vivo.
CC {ECO:0000305}.
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DR EMBL; M90498; AAC32035.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67596.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48217.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77501.1; -; Genomic_DNA.
DR PIR; A65184; A65184.
DR RefSeq; WP_000941517.1; NZ_SSZK01000025.1.
DR RefSeq; YP_026259.1; NC_000913.3.
DR AlphaFoldDB; P25550; -.
DR SMR; P25550; -.
DR BioGRID; 4259322; 5.
DR STRING; 511145.b3800; -.
DR PaxDb; P25550; -.
DR PRIDE; P25550; -.
DR DNASU; 949013; -.
DR EnsemblBacteria; AAT48217; AAT48217; b3800.
DR EnsemblBacteria; BAE77501; BAE77501; BAE77501.
DR GeneID; 949013; -.
DR KEGG; ecj:JW5594; -.
DR KEGG; eco:b3800; -.
DR PATRIC; fig|511145.12.peg.3914; -.
DR EchoBASE; EB0088; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_10_0_6; -.
DR InParanoid; P25550; -.
DR OMA; QRRFHVM; -.
DR PhylomeDB; P25550; -.
DR BioCyc; EcoCyc:EG10090-MON; -.
DR PRO; PR:P25550; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; ISS:EcoCyc.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034491; Anaerob_Ser_sulfatase-maturase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR PANTHER; PTHR43273; PTHR43273; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDF00285; anaerobic_Ser-type_sulfatase-m; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..411
FT /note="Anaerobic sulfatase-maturating enzyme homolog AslB"
FT /id="PRO_0000134459"
FT DOMAIN 3..250
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 27
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 276
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 282
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 297
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 339
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 342
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 352
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 371
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT CONFLICT 116..117
FT /note="CA -> WP (in Ref. 2; AAA67596)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="L -> C (in Ref. 2; AAA67596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46513 MW; E819FE44BE9501AA CRC64;
MLQQVPTRAF HVMAKPSGSD CNLNCDYCFY LEKQSLYREK PVTHMDDDTL EAYVRHYIAA
SEPQNEVAFT WQGGEPTLLG LAFYRRAVAL QAKYGAGRKI SNSFQTNGVL LDDEWCAFLA
EHHFLVGLSL DGPPEIHNQY RVTKGGRPTH KLVMRALTLL QKHHVDYNVL VCVNRTSAQQ
PLQVYDFLCD AGVEFIQFIP VVERLADETT ARDGLKLHAP GDIQGELTEW SVRPEEFGEF
LVAIFDHWIK RDVGKIFVMN IEWAFANFVG APGAVCHHQP TCGRSVIVEH NGDVYACDHY
VYPQYRLGNM HQQTIAEMID SPQQQAFGED KFKQLPAQCR SCNVLKACWG GCPKHRFMLD
ASGKPGLNYL CAGYQRYFRH LPPYLKAMAD LLAHGRPASD IMHAHLLVVS K
