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Database: UniProt
Entry: A0A091DMI4_FUKDA
LinkDB: A0A091DMI4_FUKDA
Original site: A0A091DMI4_FUKDA 
ID   A0A091DMI4_FUKDA        Unreviewed;       512 AA.
AC   A0A091DMI4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Pantetheinase {ECO:0000256|ARBA:ARBA00039352};
DE            EC=3.5.1.92 {ECO:0000256|ARBA:ARBA00039042};
DE   AltName: Full=Pantetheine hydrolase {ECO:0000256|ARBA:ARBA00043080};
DE   AltName: Full=Vascular non-inflammatory molecule 1 {ECO:0000256|ARBA:ARBA00041612};
GN   ORFNames=H920_06385 {ECO:0000313|EMBL:KFO32282.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO32282.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO32282.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO32282.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Amidohydrolase that hydrolyzes specifically one of the
CC       carboamide linkages in D-pantetheine thus recycling pantothenic acid
CC       (vitamin B5) and releasing cysteamine. {ECO:0000256|ARBA:ARBA00037598}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantetheine + H2O = (R)-pantothenate + cysteamine;
CC         Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753,
CC         ChEBI:CHEBI:29032, ChEBI:CHEBI:58029; EC=3.5.1.92;
CC         Evidence={ECO:0000256|ARBA:ARBA00036605};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000256|ARBA:ARBA00008225}.
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DR   EMBL; KN122191; KFO32282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091DMI4; -.
DR   STRING; 885580.ENSFDAP00000013757; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07567; biotinidase_like; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   InterPro; IPR012101; Biotinidase-like_euk.
DR   InterPro; IPR040154; Biotinidase/VNN.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR043957; Vanin_C.
DR   PANTHER; PTHR10609; BIOTINIDASE-RELATED; 1.
DR   PANTHER; PTHR10609:SF16; PANTETHEINASE; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF19018; Vanin_C; 1.
DR   PIRSF; PIRSF011861; Biotinidase; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..512
FT                   /note="Pantetheinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001872101"
FT   DOMAIN          31..307
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   ACT_SITE        80
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011861-1"
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011861-1"
FT   ACT_SITE        212
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011861-1"
SQ   SEQUENCE   512 AA;  56825 MW;  9F5F2C7EBAD39056 CRC64;
     MIPSQLFVSA AFSVFCVAKV ISLDTFIAAV YEHAVILPNA IPTPVSPEEA LALMNRNLDL
     LEGAITAAAK QGAHIIVTPE DGIYGVNFTR DSIYPYLEDI PGPQVNWIPC DNPNRFGHTP
     VQERLSCLAK DNAIYVVANI GDKKPCNSSD PQCPPHGRYQ YNTNVVFDSQ GKLVARYHKQ
     NLFMGEEQFD TPKEVEIVTF DTAFGKFGIF TCFDILFHDP AVTLVKDFHV NTILFPAAWM
     NVLPHLSAIE FHSAWAMGMG VNFLASNLHN PLKRMTGSGI YAPDFPRRFH YDMKTKEGKL
     LLSQLDSRPY RPTVNWTSYA SGIEALPTGS QGFKGTVFFD EYIFVELKGI TGNYTVCQKD
     LCCHLSYQMS EKRSDEVYAL GAFDGLHTAE GCYYLQICTL LKCKTTDLKS CGGSVDTAAT
     RFEAFSLSGT FGTQYVFPEV LLSEVQLAPG EFQVTSDGRL LSLRPTSRPV LTVTLFGRLY
     DKDETNGSPR LTAAMPRVLL MVITSVVYSL CW
//
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