ID B2HKB9_MYCMM Unreviewed; 383 AA.
AC B2HKB9;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Probable hercynylcysteine sulfoxide lyase {ECO:0000256|HAMAP-Rule:MF_02038};
DE EC=4.4.-.- {ECO:0000256|HAMAP-Rule:MF_02038};
GN Name=csdB {ECO:0000313|EMBL:ACC43616.1};
GN Synonyms=egtE {ECO:0000256|HAMAP-Rule:MF_02038};
GN OrderedLocusNames=MMAR_5211 {ECO:0000313|EMBL:ACC43616.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43616.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC43616.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- FUNCTION: Probably catalyzes the conversion of hercynylcysteine
CC sulfoxide to ergothioneine. {ECO:0000256|HAMAP-Rule:MF_02038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H(+) + S-(hercyn-2-yl)-L-cysteine S-oxide = A +
CC ergothioneine + NH4(+) + pyruvate; Xref=Rhea:RHEA:42688,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:82706,
CC ChEBI:CHEBI:134344; Evidence={ECO:0000256|HAMAP-Rule:MF_02038};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02038};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02038}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. EgtE subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02038}.
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DR EMBL; CP000854; ACC43616.1; -; Genomic_DNA.
DR RefSeq; WP_012396723.1; NC_010612.1.
DR AlphaFoldDB; B2HKB9; -.
DR STRING; 216594.MMAR_5211; -.
DR KEGG; mmi:MMAR_5211; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_1_11; -.
DR OrthoDB; 9808002at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:1990411; F:hercynylcysteine sulfoxide lyase activity (ergothioneine-forming); IEA:RHEA.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_02038; EgtE; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR027563; EgtE.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04343; egtE_PLP_lyase; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02038, ECO:0000313|EMBL:ACC43616.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02038};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT DOMAIN 21..368
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02038"
SQ SEQUENCE 383 AA; 40326 MW; E64C85EFEDDC96A3 CRC64;
MTDTLADRWR AARPPAAGLH LDSAACSRQS LEVLQAVAAH GLHEAEVGGY VAAEAAAPVL
DAGRAAVATL CGVPDARVVF TTGSLHALDL LLGSWPRESR TLACLPGEYG PNLAVMAAHG
FEVRLLPTLD DGRLALDDAA YELEEDPPEL VHLTPVASHR GTVQPLAMMA ELCRELGLPL
VVDAAQGMGQ IDCAVGADVT YSSSRKWLAG PRGVGVLAMR PEVLDRLTPR LAPPDWSPDS
PSTSVAQILE FGEANIAARV GFSLAVGEHL EYGPALIRAR LAELGAAARR VLADVDGWLV
VEEVDEPSAI TTLAPIDGAD PAAVREWLLE QRRILTTYAG IARAPQELTA PVLRVAPHVD
TTAEDLENFA EALIEATAAT TAT
//
