ID A0A087R6D3_APTFO Unreviewed; 488 AA.
AC A0A087R6D3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Pantetheinase {ECO:0000313|EMBL:KFM09037.1};
DE Flags: Fragment;
GN ORFNames=AS27_14845 {ECO:0000313|EMBL:KFM09037.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM09037.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM09037.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM09037.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC BTD/VNN family. {ECO:0000256|ARBA:ARBA00008225}.
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DR EMBL; KL226140; KFM09037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R6D3; -.
DR STRING; 9233.A0A087R6D3; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
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:SF27; CN HYDROLASE DOMAIN-CONTAINING PROTEIN; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..488
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001828490"
FT DOMAIN 40..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"
FT NON_TER 488
FT /evidence="ECO:0000313|EMBL:KFM09037.1"
SQ SEQUENCE 488 AA; 54522 MW; E482AB8FCE63C456 CRC64;
MLPSQPLLHA AVFALAVLQA LASDTFTAAV YEHAVILPDA TGEPVSPDDA LALMNKNMDV
LEGAIKEAAQ QGAHIIVTPE DGIYGWHFTR ETIYPYLEDI PDPVVNWIPC TDPTIFAPAP
VQERLSCMAR NNSIYVVANI GDKKPCNSSD AGCPSDGRYQ YNTDVVFDPE GKLVARYHKY
NLFMSETQFN YPKEPEAVTF ETPFGKFGIF TCFDILFREP AVVLVSELQV DTVLFPTAWM
NVLPFLTAVE FHSAWAMGMG VNFLAANTHY TSMSMTGSGI YAPDGARTYY YNMKTEDGRL
LIAELDSHPR LSPASPPAVN WSSYALSVER FSPNDHDFRG CIFYDWFTFT EVTKPEWNLT
VCQKDLCCHL SYKVAEKQED EVYVLGAFDG LHVVEGQYYL QICTLLKCKT TDLNTCGQPV
ETAQTKFETF SLSGTFGTNY VFPEVLYSGV QLAPGEFEVL NDGRLISKTR PTKPVVTVTL
FGRWYEKD
//
