ID A0A0B7H464_9FLAO Unreviewed; 620 AA.
AC A0A0B7H464;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Leukotriene A(4) hydrolase {ECO:0000313|EMBL:CEN33319.1};
DE EC=3.4.11.2 {ECO:0000313|EMBL:CEN33319.1};
GN ORFNames=CCYN2B_160012 {ECO:0000313|EMBL:CEN33319.1};
OS Capnocytophaga cynodegmi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=28189 {ECO:0000313|EMBL:CEN33319.1, ECO:0000313|Proteomes:UP000038055};
RN [1] {ECO:0000313|Proteomes:UP000038055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ccyn2B {ECO:0000313|Proteomes:UP000038055};
RA MANFREDI Pablo;
RL Submitted (JAN-2015) 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};
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DR EMBL; CDOD01000008; CEN33319.1; -; Genomic_DNA.
DR RefSeq; WP_041990790.1; NZ_CDOD01000008.1.
DR AlphaFoldDB; A0A0B7H464; -.
DR STRING; 28189.CCYN74_30056; -.
DR eggNOG; COG0308; Bacteria.
DR Proteomes; UP000038055; 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; cd09604; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:CEN33319.1};
KW Hydrolase {ECO:0000313|EMBL:CEN33319.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW Protease {ECO:0000313|EMBL:CEN33319.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000038055};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002117042"
FT DOMAIN 349..504
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 445
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 620 AA; 71605 MW; 478A5DD63309EA08 CRC64;
MNKYIFAVFL LGVFTFSKAQ NTSYWQQQAD YEMEIDMDVK NFQYKGKQKL TYTNNSPDTL
QVVFYHLYLN AFQPGSEMDA RLQSITDPDR RMVINKGTKE NPIYESRIAS LKPNEIGYIH
VKSLTQNGES VSHKTEGTIL KVNLKNPILP NSKVIFDMEF EAQVPVMIRR TGRNSRDGVA
ISMAQWYPKI AAYDYRGWHP TEYIAREFYG VWGNFDVKIT IDKNYILGGS GVLQNNNEIG
FGYENEGVKV PKAKGKTKTW HFIAKNVHDF TWVADMEFKH DKVALKDGKV FHFLYKKYDE
NWRKMQPELV KVFDFFNEVI GKYPWEQYSF IQGGDGGMEY AMCTLVAGGE KYESVLGTSI
HELAHAWFQH LLATDESAYA WMDEGFTSFI EDLAMHSIIS PDSKGNPFQN SYASYYELVK
SGLEEPATTH ADRFDKNFSY SVMAYGKGLL FLTQLGYIMG EQNVIKSLQK FYKDFAFKNP
TPNDFIRTAE KVSGMQLQWF LNEFIGTTHT ADYAIESVKP KGNKTEITLR RIGRLPLPVD
LFVIEKSEKI HYYHIPLRMT FGSKENPYKS YQQHILSSWG WGNMTYTFEV DLPMQEVKSI
IVDPTNISVD INKENNIFNN
//
