ID A0A068S070_9FUNG Unreviewed; 378 AA.
AC A0A068S070;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LCOR_06891.1 {ECO:0000313|EMBL:CDH55778.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH55778.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH55778.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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 -!- 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:CDH55778.1}.
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DR EMBL; CBTN010000032; CDH55778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S070; -.
DR STRING; 1263082.A0A068S070; -.
DR VEuPathDB; FungiDB:LCOR_06891.1; -.
DR OrthoDB; 47357at2759; -.
DR Proteomes; UP000027586; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT DOMAIN 5..176
FT /note="Isochorismatase-like"
FT /evidence="ECO:0000259|Pfam:PF00857"
SQ SEQUENCE 378 AA; 42600 MW; A3E1F434324875EB CRC64;
MAPVALLLVD IQNDFMENGS LAVPNASQIM PVVLRLISDT KDRIVVASKD WHPSNHISFA
SNHADKQPFE QIRIEYRGRE SQQVLWPAHC VQGSTGAELA KDIPSDKVDY IVNKGQNNHV
DSYSAFADND YHEITSLAKI LYQNFVDTVI VVGLAADYCV KMTSLDAVKF GFKTILRLYE
NDVDQHDREN LLTKFRGRHG QYRRARPHAL FMLSSIHRLS HIQGFHNELW GPCGNEIAQH
DRENLLTKFQ CAWICGAVPD LSNFQLFHSQ PLVSFLPILN CCPIQVERQP ANDCPPSTHH
DKPTIALTER QVPGVCTPRL HTPSLILHML LYTRLPQSNV TAFIPVAAIS EALAPLSSSY
LQQHALQPLL RRQQIAII
//
