EGT2_NEUCR
ID EGT2_NEUCR Reviewed; 473 AA.
AC A7UX13;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Hercynylcysteine sulfoxide lyase {ECO:0000305|PubMed:25275953};
DE EC=4.4.1.- {ECO:0000269|PubMed:25275953};
DE AltName: Full=Ergothioneine biosynthesis protein 2 {ECO:0000250|UniProtKB:O94431};
DE AltName: Full=PLP-binding cysteine desulfurase {ECO:0000250|UniProtKB:O94431};
DE AltName: Full=PLP-dependent C-S lyase {ECO:0000303|PubMed:25275953};
GN Name=egt-2 {ECO:0000303|PubMed:25275953}; ORFNames=NCU11365;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=25275953; DOI=10.1021/ol502596z;
RA Hu W., Song H., Sae Her A., Bak D.W., Naowarojna N., Elliott S.J., Qin L.,
RA Chen X., Liu P.;
RT "Bioinformatic and biochemical characterizations of C-S bond formation and
RT cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic
RT pathway.";
RL Org. Lett. 16:5382-5385(2014).
CC -!- FUNCTION: Catalyzes the conversion of hercynylcysteine sulfoxide to
CC ergothioneine by cleaving the cysteine residue at the sulfur atom, the
CC last step in the biosynthesis pathway of ergothioneine.
CC {ECO:0000269|PubMed:25275953}.
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:0000269|PubMed:25275953};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:25275953};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=194.7 uM for S-(hercyn-2-yl)-L-cysteine S-oxide
CC {ECO:0000269|PubMed:25275953};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000305|PubMed:25275953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O94431}. Nucleus
CC {ECO:0000250|UniProtKB:O94431}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. EgtE subfamily. {ECO:0000305}.
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DR EMBL; CM002239; EDO65040.1; -; Genomic_DNA.
DR RefSeq; XP_001728131.1; XM_001728079.2.
DR PDB; 5UTS; X-ray; 2.30 A; A/B/C/D/E/F/G/H=2-473.
DR PDB; 5V12; X-ray; 2.45 A; A/B/C/D/E/F/G/H=2-473.
DR PDB; 5V1X; X-ray; 2.56 A; A/B/C/D/E/F/G/H=2-473.
DR PDBsum; 5UTS; -.
DR PDBsum; 5V12; -.
DR PDBsum; 5V1X; -.
DR AlphaFoldDB; A7UX13; -.
DR SMR; A7UX13; -.
DR STRING; 5141.EFNCRP00000007711; -.
DR EnsemblFungi; EDO65040; EDO65040; NCU11365.
DR GeneID; 5847244; -.
DR KEGG; ncr:NCU11365; -.
DR VEuPathDB; FungiDB:NCU11365; -.
DR HOGENOM; CLU_003433_3_0_1; -.
DR InParanoid; A7UX13; -.
DR OMA; DDHRANG; -.
DR BRENDA; 4.4.1.36; 3627.
DR SABIO-RK; A7UX13; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990411; F:hercynylcysteine sulfoxide lyase activity (ergothioneine-forming); IEA:RHEA.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Nucleus; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..473
FT /note="Hercynylcysteine sulfoxide lyase"
FT /id="PRO_0000434988"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23721"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:5UTS"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:5UTS"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5UTS"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5V12"
FT HELIX 311..325
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 330..352
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5V12"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:5V12"
FT HELIX 390..395
FT /evidence="ECO:0007829|PDB:5UTS"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5V12"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 407..420
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:5UTS"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:5UTS"
FT HELIX 447..465
FT /evidence="ECO:0007829|PDB:5UTS"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:5V12"
SQ SEQUENCE 473 AA; 53015 MW; 5C44B48F81CC18AD CRC64;
MVATTVELPL QQKADAAQTV TGPLPFGNSL LKEFVLDPAY RNLNHGSFGT IPSAIQQKLR
SYQTAAEARP CPFLRYQTPV LLDESRAAVA NLLKVPVETV VFVANATMGV NTVLRNIVWS
ADGKDEILYF DTIYGACGKT IDYVIEDKRG IVSSRCIPLI YPAEDDDVVA AFRDAIKKSR
EEGKRPRLAV IDVVSSMPGV RFPFEDIVKI CKEEEIISCV DGAQGIGMVD LKITETDPDF
LISNCHKWLF TPRGCAVFYV PVRNQHLIRS TLPTSHGFVP QVGNRFNPLV PAGNKSAFVS
NFEFVGTVDN SPFFCVKDAI KWREEVLGGE ERIMEYMTKL AREGGQKVAE ILGTRVLENS
TGTLIRCAMV NIALPFVVGE DPKAPVKLTE KEEKDVEGLY EIPHEEANMA FKWMYNVLQD
EFNTFVPMTF HRRRFWARLS AQVYLEMSDF EWAGKTLKEL CERVAKGEYK ESA
