(data stored in SCRATCH zone)

SWISSPROT: A4DA77_ASPFU

ID   A4DA77_ASPFU            Unreviewed;       443 AA.
AC   A4DA77;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   SubName: Full=Cystathionine beta-lyase MetG {ECO:0000313|EMBL:EBA27192.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:EBA27192.1};
GN   ORFNames=AFUA_4G03950 {ECO:0000313|EMBL:EBA27192.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EBA27192.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EBA27192.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EBA27192.1}.
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DR   EMBL; AAHF01000016; EBA27192.1; -; Genomic_DNA.
DR   RefSeq; XP_001481546.1; XM_001481496.1.
DR   STRING; 746128.CADAFUBP00009626; -.
DR   EnsemblFungi; EBA27192; EBA27192; AFUA_4G03950.
DR   GeneID; 5077098; -.
DR   KEGG; afm:AFUA_4G03950; -.
DR   EuPathDB; FungiDB:Afu4g03950; -.
DR   HOGENOM; HOG000246415; -.
DR   InParanoid; A4DA77; -.
DR   KO; K01760; -.
DR   OMA; AVDNCFC; -.
DR   OrthoDB; 572061at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR   GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006238; Cys_b_lyase_euk.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01329; cysta_beta_ly_E; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4DA77.
DR   SWISS-2DPAGE; A4DA77.
KW   Lyase {ECO:0000313|EMBL:EBA27192.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   443 AA;  47744 MW;  5DE91A5C546F4074 CRC64;
     MSASGSGAAV PAATDVMKKA FPHVDLDGHN LPPSPAPSSP RTGKRYAIAT ELVYTDSNDQ
     YNASSVPIYQ SATFKQTSGG GGGEYDYTRS GNPTRTHLER HLAKIMSAQR ALVVSSGMAA
     LDVISRLLRP GDEVVTGDDL YGGTHRLLKY LSTNGGIIVH HVDTTQPEKV REVLTPKTAM
     VLLETPTNPL IKIVDIPQIA TAAHEVNPSC LVAVDNTMMS PLLLNPLELG ADIVYESGTK
     YLSGHHDLMA GVIAVNDLAL GERLYFPINA SGCGLSPFDS WLLMRGVKTL KVRMDQQQSN
     AQRIAEFLEA HGFKVRYPGL RSHPQYELHH SMARGAGAVL SFETGDVAVS ERIVESAKLW
     AISVSFGCVN SLISMPCRMS HASIDAKTRQ ERAMPEDLIR LCVGIEDVDD LIDDLRRALV
     QAGAVNITLD GFEANASNET NSA
//

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