ID A0A0U9HN94_KLENI Unreviewed; 591 AA.
AC A0A0U9HN94;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Leukotriene-A4 hydrolase {ECO:0000313|EMBL:GAQ90050.1};
GN ORFNames=KFL_005930070 {ECO:0000313|EMBL:GAQ90050.1};
OS Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ90050.1, ECO:0000313|Proteomes:UP000054558};
RN [1] {ECO:0000313|EMBL:GAQ90050.1, ECO:0000313|Proteomes:UP000054558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ90050.1,
RC ECO:0000313|Proteomes:UP000054558};
RX PubMed=24865297; DOI=10.1038/ncomms4978;
RA Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA Tabata S., Ida S., Kurokawa K., Ohta H.;
RT "Klebsormidium flaccidum genome reveals primary factors for plant
RT terrestrial adaptation.";
RL Nat. Commun. 5:3978-3978(2014).
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; DF237542; GAQ90050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U9HN94; -.
DR STRING; 105231.A0A0U9HN94; -.
DR OrthoDB; 443480at2759; -.
DR Proteomes; UP000054558; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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, ECO:0000313|EMBL:GAQ90050.1};
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:UP000054558};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 447..585
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 284
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 371
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 125..127
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 254..259
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 540..542
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ SEQUENCE 591 AA; 65101 MW; 577343ADB37ABD62 CRC64;
MGFIDPHSFA DVDQPLVKSV ALELRLDFDS KTINATADYV LKSAASGTLD FDTRDLGVEA
VTGEGGESVA FDTDHKDAIK GQRLRMHLHG SRLFIRYRIP PSASALQWLE PAMTAGGKLP
FVFTQCQPIH ARSLFPCQDT PAARISYAAR VEVPKELHVV MSAVHLGREE RGATAFEVFA
TEEPIPPYLF AFAAGELQRQ DLGPRSAVYA EPSMLQAAAR EFEDVEAMIS AAEALFGPYK
WGRFDMLLMP PSFPYGGMEN PRMAFMTPTL ITGDKSLVNV VAHELAHSWT GNLVTNATMD
HFWLNEGFTV YAERRILEAT EGPERVAFHA AIGYAGLLEE LERFGPDSEY TKLRMNLEGV
DPDDVFSDVP YEKGFLFLRH LETAVGRPAF DAFLQAYIAH FQFQSIDTAT FLAFLHARLP
GLPPSLDLPA WIDAPGLPSN APVPRSAALD KVKSLAAAFP SGARLSEEDH RGWQYLEWQT
FLDALPKRLP AADVAWLEDH FQLAAAPNPE IRITFLVIAA HSDYQPAFPA IHEALLTLGR
MKYLKPLYAG LLAGSPDGHA LASRTFATAA PKYHPIARTV IQGLLDKAAT R
//
