ID A0A0D8FUQ1_9ACTN Unreviewed; 319 AA.
AC A0A0D8FUQ1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Proline iminopeptidase {ECO:0000313|EMBL:KJE75982.1};
DE EC=3.4.11.5 {ECO:0000313|EMBL:KJE75982.1};
GN Name=fpaP {ECO:0000313|EMBL:KJE75982.1};
GN ORFNames=FEAC_22790 {ECO:0000313|EMBL:KJE75982.1};
OS Ferrimicrobium acidiphilum DSM 19497.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrimicrobium.
OX NCBI_TaxID=1121877 {ECO:0000313|EMBL:KJE75982.1, ECO:0000313|Proteomes:UP000032336};
RN [1] {ECO:0000313|EMBL:KJE75982.1, ECO:0000313|Proteomes:UP000032336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T23 {ECO:0000313|EMBL:KJE75982.1,
RC ECO:0000313|Proteomes:UP000032336};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Ferrimicrobium acidiphilum
RT strain T23.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR005539}.
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:KJE75982.1}.
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DR EMBL; JXUW01000024; KJE75982.1; -; Genomic_DNA.
DR RefSeq; WP_035390279.1; NZ_JXUW01000024.1.
DR AlphaFoldDB; A0A0D8FUQ1; -.
DR STRING; 1121877.FEAC_22790; -.
DR GeneID; 78373330; -.
DR PATRIC; fig|1121877.4.peg.2537; -.
DR eggNOG; COG2267; Bacteria.
DR OrthoDB; 9801162at2; -.
DR Proteomes; UP000032336; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005945; Pro_imino_pep.
DR NCBIfam; TIGR01250; pro_imino_pep_2; 1.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR PANTHER; PTHR43798:SF31; NON-HEME BROMOPEROXIDASE BPOC-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:KJE75982.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR005539, ECO:0000313|EMBL:KJE75982.1};
KW Protease {ECO:0000313|EMBL:KJE75982.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032336}.
FT DOMAIN 48..302
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 296
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
SQ SEQUENCE 319 AA; 36164 MW; CBD82757CF5F473C CRC64;
MASENSYLDY SSRNDRLSGG ARRIPIETPA GSFYVWTKRV GNNPKLKVLL LHGGPGANHA
YFEAVDSYFP ASGIEYYYYD QLGSIFSDQP NEPSLWEIDR FVDEVEQVRY ALGLDRDNFV
LLGHSWGGIL AIEYALAHQD HLRGLVISNM MASAPAYTAY AEQVLMPQMD QDALSEIKAI
EAAGDIDNPR YMELLIPHFY EYHTLRMPAA EWPDPVQRGF DHINQQIYVS MQGPSELGMS
ADAKLAAWDR VNDLEKIMVP TLVIGARYDT MDPAHMEMMS ERLPRGHYLY CPNGSHMALY
DDQQTYFAGL VDFLRQLPS
//
