ID A0A372JHB7_9ACTN Unreviewed; 402 AA.
AC A0A372JHB7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:RFU38758.1};
DE EC=3.4.11.1 {ECO:0000313|EMBL:RFU38758.1};
DE Flags: Fragment;
GN ORFNames=DZF91_25990 {ECO:0000313|EMBL:RFU38758.1};
OS Actinomadura logoneensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2293572 {ECO:0000313|EMBL:RFU38758.1, ECO:0000313|Proteomes:UP000261811};
RN [1] {ECO:0000313|EMBL:RFU38758.1, ECO:0000313|Proteomes:UP000261811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-G17 {ECO:0000313|EMBL:RFU38758.1,
RC ECO:0000313|Proteomes:UP000261811};
RA Shi L.;
RT "Actinomadura jelena sp. nov., a novel Actinomycete isolated from soil in
RT Chad.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC but not glutamic or aspartic acids.; EC=3.4.11.10;
CC Evidence={ECO:0000256|ARBA:ARBA00000967};
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:RFU38758.1}.
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DR EMBL; QURH01000709; RFU38758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372JHB7; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000261811; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:RFU38758.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RFU38758.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261811}.
FT DOMAIN 244..251
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU38758.1"
SQ SEQUENCE 402 AA; 41022 MW; C3448DE1687BAAEF CRC64;
EGLRRAAGAA LRALAGKTRV AVALPAASAE ELEAVALGAL LGNYGFTAYR TSERPGPVGE
IVLVGSGDEA AVRRAETLAS AVSLVRDLVN TPPSDLSPED FAGVATKVAS EGGLDIEVLD
EKALVDGGYG GIVGVGQGSA NPPRLVRLAY THPEASKTLA LVGKGITFDS GGLSLKPAEG
MDWMKSDMGG AAAVLGALAA IAELKPAVNV VGYLALAENM PSGTAQRPSD VLTVYGGKTV
EVLNTDAEGR LVMADPIVRS GEDGPDLLID VATLTGAQLV ALGTRTTGVM ANDDEVREKV
VAAAVRSGEP SWGMPLPEEL RKGLDSAVAD IANISGERWG GMLVAGVFLK EFVPDGVRWA
HLDIAGPSYN KGEPYGYTPK AGTGAAVRTL VAVAEDMAAG EL
//
