ID A0A100IBK2_ASPNG Unreviewed; 518 AA.
AC A0A100IBK2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=cysteine dioxygenase {ECO:0000256|ARBA:ARBA00013133};
DE EC=1.13.11.20 {ECO:0000256|ARBA:ARBA00013133};
GN ORFNames=ABL_02541 {ECO:0000313|EMBL:GAQ38219.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ38219.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00006622}.
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:GAQ38219.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BCMY01000003; GAQ38219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IBK2; -.
DR PaxDb; 5061-CADANGAP00004339; -.
DR VEuPathDB; FungiDB:An04g07220; -.
DR VEuPathDB; FungiDB:An04g07230; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1187214; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_214187; -.
DR VEuPathDB; FungiDB:ATCC64974_81980; -.
DR VEuPathDB; FungiDB:ATCC64974_81990; -.
DR VEuPathDB; FungiDB:M747DRAFT_299417; -.
DR VEuPathDB; FungiDB:M747DRAFT_318619; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd10548; cupin_CDO; 1.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR010300; CDO_1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR12918; CYSTEINE DIOXYGENASE; 1.
DR PANTHER; PTHR12918:SF1; CYSTEINE DIOXYGENASE TYPE 1; 1.
DR Pfam; PF05995; CDO_I; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR610300-51};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR610300-51};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT DOMAIN 14..220
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 417
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 419
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 474
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT CROSSLNK 424..491
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ SEQUENCE 518 AA; 58032 MW; 501A766078372941 CRC64;
MEPIIHPIFE KQTSTWQYIV ACPETHEAVI IDPVLDFDPT QLTVTTTSAD ELLDFAASKG
YHITRILETH AHADHLTAAH YIQTKLHHQQ RSSLSSSSST ESSPKVPICT GHRIRQVQAT
FAQRYNIPSN DLDTAFDHLF QDDETFQIGR ITAQVLHLPG HTPDHSGYMI GSNVFTGDSI
FNPDVGSARC DFPHGDARAL YQSMRKLLAL PEHVKLYTGH DYPPADSTTN RAPKAFVTVK
DQKEGNKHVK EGTGEEEFVK WRQERDAALG EPRLLHPSLQ VNVRGTKLST FNIYILVTTM
ASTMLASFPG SAASYTTSHL SKDSAPLLVE EDNYTFEQLV HDLRSYLGSS RGIDGENVDH
KVLIAFMSKY ASNPKDWSRF ARNDVSKNYT RNLVEDINGR ANLLVLVWNP QKGSPIHDHA
DAHCIMKILG GELNEVIYDT PDPERGHDAP LTVKQETTYK TDEVAYICDQ IGLHRVMNPR
KDQVAVSLHL YTPPNAADFG YNIYDRDTGR SSHVYQAS
//
