ID A0A1H9EPX2_9GAMM Unreviewed; 860 AA.
AC A0A1H9EPX2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=SAMN04488038_105112 {ECO:0000313|EMBL:SEQ27662.1};
OS Solimonas aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Solimonas.
OX NCBI_TaxID=489703 {ECO:0000313|EMBL:SEQ27662.1, ECO:0000313|Proteomes:UP000199233};
RN [1] {ECO:0000313|EMBL:SEQ27662.1, ECO:0000313|Proteomes:UP000199233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25927 {ECO:0000313|EMBL:SEQ27662.1,
RC ECO:0000313|Proteomes:UP000199233};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; FOFS01000005; SEQ27662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9EPX2; -.
DR STRING; 489703.SAMN04488038_105112; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000199233; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000199233};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..860
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011457725"
FT DOMAIN 31..209
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 244..459
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 532..838
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 402
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 860 AA; 95200 MW; 5D741CB6BC257F79 CRC64;
MKQWLAGLAV LLWAQAGIAA PSREQLPTTA QPLLYELELR PDAQALRFTA QLGVTLEIRQ
ATSRLELNAA ELQIAQASLD GQPARHIRLD AERQRLILDF ARPLTPGRHR LQIAYAGRIN
TQPAGLFALD YATAQGQQRA LYTQFEPADA RRLLPCWDEP GIKARYTLSA VLPQAQMAVS
NMPVAEQTPA GDGLKRVRFE TSPLMSSYLL FFAAGDFERQ SRMVEGVDLG VVVRRGELGR
AQEALETAAQ VLPYYNDYFG VKFPLPKLDM IAAAGSSVSF SAMENWGAIL YFESAMLLDA
QTSTTADRRE VFAVIAHEMA HQWFGNLVTM QWWDDLWLNE GFAEWMQSKA AERLHPDWHV
WLDAQGERSG AMDLDARSSA HAVVQAVADS RQADQAFDDI TYRKGQAVIR MLEQWLGADV
FRDGVRRYFA AHAYGNATTD ALWSALAQAA GQPVVHVAHG FTLQPGVPMI EASRSGEALR
LQLSRYGVDD SRKRPPPWQV PVKVASLSAG GEDWQGLVAR QPQMLPHIEL PLVNAGQSGY
FRTRYQSQLL DALLPQFAQL SLADQYGLLD DSLALGYSGD QPLSDFLRIA AQCPPGSHPL
IVSALTRRLM RLDDAYRGLP AQAAYRRRAI ALLQPLLAAV GWDARAGEDG NTPLARSSLI
SALGQFGDAA VIATANARYR HWLEQPQTLS GEARDDVLNV VVRNAGAGDW ALLQAARQQA
GSELDAQHLR FALTGVRDPA LVRRMLEEVL HGQLPTTERS AMMQALAYQQ PELVFDFVLR
NIEAVHDLLE PSARDRFVPD LAAHSADPAL IARLRQYAAR YIPASAQQSV REAEAAIRFH
ARLRRERLPA LTRYLAQQDS
//
