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Database: UniProt
Entry: A4BVX3_9FLAO
LinkDB: A4BVX3_9FLAO
Original site: A4BVX3_9FLAO 
ID   A4BVX3_9FLAO            Unreviewed;       549 AA.
AC   A4BVX3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Aminopeptidase M1 family protein {ECO:0000313|EMBL:EAR13114.1};
GN   ORFNames=PI23P_01432 {ECO:0000313|EMBL:EAR13114.1};
OS   Polaribacter irgensii 23-P.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR13114.1, ECO:0000313|Proteomes:UP000003053};
RN   [1] {ECO:0000313|EMBL:EAR13114.1, ECO:0000313|Proteomes:UP000003053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23-P {ECO:0000313|EMBL:EAR13114.1,
RC   ECO:0000313|Proteomes:UP000003053};
RA   Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
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:EAR13114.1}.
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DR   EMBL; AAOG01000001; EAR13114.1; -; Genomic_DNA.
DR   RefSeq; WP_004568906.1; NZ_CH724148.1.
DR   AlphaFoldDB; A4BVX3; -.
DR   STRING; 313594.PI23P_01432; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_014298_1_1_10; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000003053; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09603; M1_APN_like; 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; IPR034015; M1_LTA4H.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:EAR13114.1};
KW   Hydrolase {ECO:0000313|EMBL:EAR13114.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW   Protease {ECO:0000313|EMBL:EAR13114.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003053};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..549
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002665630"
FT   DOMAIN          52..219
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          271..473
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        339
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        413
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   549 AA;  63440 MW;  35827A501156AEBF CRC64;
     MKHPFYLHLF FIVICSLNLQ AQGLLTEKDI FSRQDTLRGS ITPERVWWDL TYYHLEVTVA
     PDKKYISGKN TIKYTVLNVY QTMQIDLQTP LQMTKVTQDG KELAIIHEGN AHFIKLTKAQ
     VIGNTESIIV HYESNPKEAV NAPWDGGFSW KKDKNGNHFI ATSCQGLGAS VWWPCKDHMY
     DEVKSMRISV TVPSHLMDVS NGRLESIEDH GTTKTYNWFV NNPINNYGVN VNIGDYTHFS
     ETFDGEKGPL DMDYYVLKYN LAKAKKQFTD APKMMKAFEH WFGPYPFYKD GYKLVEVPYL
     GMEHQSSVTY GNEFKQGYLG SDLSGTGWGL KFDFIIIHES GHEWFANNIT DIDAADMWIH
     ESFTNYSESL FLDYYYGKKA ASEYVIGLRK SIANKTPIIG TYNVNKSGSS DMYNKGGNLL
     HTLRQLIDND KKWRLILRKM NAQFYHQTVK TKQIEDFLST ETGFDLNPFF NQYLRTIKIP
     TLAHKIENDT LKYRWTNTVP NFEMPLKTTI NGKEKWIYPA SNWKSLALKS AGTSFLIDEN
     FYVFNKKVD
//
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