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Database: UniProt
Entry: K5XJ38_AGABU
LinkDB: K5XJ38_AGABU
Original site: K5XJ38_AGABU 
ID   K5XJ38_AGABU            Unreviewed;       635 AA.
AC   K5XJ38;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal domain-containing protein {ECO:0000259|SMART:SM01263};
GN   ORFNames=AGABI1DRAFT_103588 {ECO:0000313|EMBL:EKM83357.1};
OS   Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS   10392) (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM83357.1, ECO:0000313|Proteomes:UP000008493};
RN   [1] {ECO:0000313|Proteomes:UP000008493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC   {ECO:0000313|Proteomes:UP000008493};
RX   PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA   Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA   Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA   Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA   Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA   Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA   Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA   Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT   "Genome sequence of the button mushroom Agaricus bisporus reveals
RT   mechanisms governing adaptation to a humic-rich ecological niche.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; JH971385; EKM83357.1; -; Genomic_DNA.
DR   RefSeq; XP_007325343.1; XM_007325281.1.
DR   AlphaFoldDB; K5XJ38; -.
DR   STRING; 597362.K5XJ38; -.
DR   MEROPS; M01.004; -.
DR   GeneID; 18821921; -.
DR   KEGG; abp:AGABI1DRAFT103588; -.
DR   eggNOG; KOG1047; Eukaryota.
DR   HOGENOM; CLU_014505_1_2_1; -.
DR   InParanoid; K5XJ38; -.
DR   OMA; CTALQWM; -.
DR   OrthoDB; 443480at2759; -.
DR   Proteomes; UP000008493; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09599; M1_LTA4H; 1.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 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; IPR016024; ARM-type_fold.
DR   InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR   InterPro; IPR034015; M1_LTA4H.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR015211; Peptidase_M1_C.
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; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM01263; Leuk-A4-hydro_C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634015-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008493};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT   DOMAIN          476..632
FT                   /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT                   C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01263"
FT   ACT_SITE        304
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        392
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         130..132
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT   BINDING         274..279
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         590..592
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ   SEQUENCE   635 AA;  71637 MW;  EDC789C2C0A86EFB CRC64;
     MDPTTQSNYD KVATEHVEFD WRLDFENRII QGSAVHQLTI KAESVHEAIF DTNDLTINGV
     SIEGKATSFD LKPKHEVMGS ALHVSLPSGL SKGAKLRVQI QYQTSPNSMA LQWLEKEQTQ
     GKQFPYLFSQ CQPIYSRALA PLQDSPSAKI TYSAKVKSVL PVLLSAIRVS PPADGPPHGG
     KIIGKDEITY SYNQPVPIAT YLIAIAAGNI HFRSFPQHEG KTWTSGIWTE PELLDAAYWE
     FSEDTTKFLA KEESLVIPYG FGVYDLLVLP PSFPYGGMEN ACLTFLTPTL VTGDRTLVDV
     VVHELTHSWF GNGVTHAEAS HFWLNEGWTT YMERVLQQFL HSPAHRGFSY LIGNRALRDA
     LEEYKDRPKY QRLIIGFEKG EDPDDAYSSI PYEKGANFLF YIEQTLGGLD VFLPYVKDYV
     STFIGKSIRT EDWKSHLYGY FKDQPDKIKA LNSIDWDAWF YGEGTELPVE LKFDTTLATQ
     AYALAKRWDE ARSTTDISRL DFKETDLQKF DANQIVVFLE KLQSYPPLPS DLILHLGSLY
     GVSSTSNAEI RLRFYGVALQ DANSPAAQHF AVEAAKWVIG DDGTGIIKGR MKFCRPTFRS
     ISKVNHDVAV ETFMKAKNYF HPIARKLIEK DLKLA
//
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