ID A0A178A9I1_9PLEO Unreviewed; 228 AA.
AC A0A178A9I1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=nicotinamidase {ECO:0000256|ARBA:ARBA00039017};
DE EC=3.5.1.19 {ECO:0000256|ARBA:ARBA00039017};
DE AltName: Full=Nicotinamide deamidase {ECO:0000256|ARBA:ARBA00043224};
GN ORFNames=IQ06DRAFT_286792 {ECO:0000313|EMBL:OAK94153.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK94153.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK94153.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK94153.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; nicotinate biosynthesis; nicotinate
CC from nicotinamide: step 1/1. {ECO:0000256|ARBA:ARBA00037900}.
CC -!- SIMILARITY: Belongs to the isochorismatase family.
CC {ECO:0000256|ARBA:ARBA00006336}.
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; KV441726; OAK94153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178A9I1; -.
DR STRING; 765868.A0A178A9I1; -.
DR InParanoid; A0A178A9I1; -.
DR OrthoDB; 47357at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019363; P:pyridine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01011; nicotinamidase; 1.
DR Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR PANTHER; PTHR11080:SF2; LD05707P; 1.
DR PANTHER; PTHR11080; PYRAZINAMIDASE/NICOTINAMIDASE; 1.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OAK94153.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 6..217
FT /note="Isochorismatase-like"
FT /evidence="ECO:0000259|Pfam:PF00857"
FT REGION 56..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 24911 MW; 3082E93E4BFE2814 CRC64;
MTFNPALVVV DVQEDFCPPH GALAVTGGRD IVPTINELLA LPFAIKVATK DFHPQDHISF
ASNHPSPNNK PFESKATIAN PHNPNETQET QLWPDHCVQG TKGAELLPEL DVGKIDHVVE
KGQDKRVEMY SAFADPFTNP RVAQSNLAQT LRDARITDVF VVGLAADYCV KFTAMDAAKE
GFKTWVIGEA TKAVDPSSLE AVYAEYEKLG VLVISKDDAQ IGKITQRT
//
