ID F9ZAR7_ODOSD Unreviewed; 844 AA.
AC F9ZAR7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN OrderedLocusNames=Odosp_3441 {ECO:0000313|EMBL:ADY34393.1};
OS Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / JCM
OS 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY34393.1, ECO:0000313|Proteomes:UP000006657};
RN [1] {ECO:0000313|EMBL:ADY34393.1, ECO:0000313|Proteomes:UP000006657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC {ECO:0000313|Proteomes:UP000006657};
RX PubMed=21677857; DOI=10.4056/sigs.1714269;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., Hammon N.,
RA Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Detter J.C., Woyke T., Bristow J., Markowitz V., Hugenholtz P.,
RA Eisen J.A., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Odoribacter splanchnicus type strain
RT (1651/6).";
RL Stand. Genomic Sci. 4:200-209(2011).
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|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; CP002544; ADY34393.1; -; Genomic_DNA.
DR RefSeq; WP_013613580.1; NZ_CP086000.1.
DR AlphaFoldDB; F9ZAR7; -.
DR STRING; 709991.Odosp_3441; -.
DR PaxDb; 709991-Odosp_3441; -.
DR GeneID; 69854150; -.
DR KEGG; osp:Odosp_3441; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_0_0_10; -.
DR OrthoDB; 100605at2; -.
DR BioCyc; OSPL709991:G1GRN-3512-MONOMER; -.
DR Proteomes; UP000006657; Chromosome.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09602; M1_APN; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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:0000313|EMBL:ADY34393.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADY34393.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006657};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..207
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 247..460
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 844 AA; 96635 MW; 02FD8DA36BFCBC13 CRC64;
MKKQLFFIIL LGVVELLAGC RPEGKEPETG VSIGLARQRK QDISNLQYRL KFRIPENKQE
EVIGKVQITL KQEKVQPVVL DFREDPHKVK QLKVNGRPDS IRISNEHIVV GTDYLKKGAN
EIEIDFIAGN QSLNRNDEFL YTLLVPERAR TLFPCFDQPD MKAVFTLQLD IPEQWVAVAN
AAVESETLHE GRKLIAFQPT QPLSTYLFSF VAGKWQQLAE SRDGKTIVMY YRETDPQKVA
QHTIIFDQVF ASLKWLEDYT GIPYPFDKYD LVIVPGFQFG GMEHPGAVLY NDKRMFLGPH
PTIEEELGRM ELIAHETTHM WFGDAVTMAW FDDVWTKEVF ANYFASQMTR PEFPGVNHLL
NDLRNFYIPA YAEDRTAGST SIKQPLENLK DAGLIYGQIV YDKAPIVMNM LLKLLGEEAF
QKGIREYLQT YLYGNATWDN LITILNKYTD KDLVAWSNSW VNEKGMPEIS ASWHDRTLVV
RQKDPWHRGL SWPQNISIAL YEGKNADTLQ SSVHEVTLVS DSAVTVFQNR SADESCIFLN
QNGEAYGYFV LDQRTIAYAL AHLNTFAKAP ETRLALLINL NENRLHGRVD GLAFARMLIS
NLKTETEPLI ISTSIAYLNE MALHGQIAGS EELEESLLGL ARKPGGKGCQ QAAFRALLGT
FRQPATTQEI YRMWKEQKSF TGLALGESDY TKMAYELAVR MPEKYEEIRA TQATRIQDPD
RKREFNFIVR AVAPETETRD SLFRSLLIAG NRRIEPWVTQ IVGYLNHPLR QQQAVKYIRP
ALQELQEVQR TGDIFFPKNW ISATLRGHNS PEAAQVVRQF LEQHPDYPVL LKNKILQSAD
HLYR
//
