APEB_AZOVD
ID APEB_AZOVD Reviewed; 429 AA.
AC C1DQM8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_00467};
DE EC=3.4.11.- {ECO:0000255|HAMAP-Rule:MF_00467};
GN Name=apeB {ECO:0000255|HAMAP-Rule:MF_00467}; OrderedLocusNames=Avin_35150;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00467};
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000255|HAMAP-
CC Rule:MF_00467}.
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DR EMBL; CP001157; ACO79664.1; -; Genomic_DNA.
DR RefSeq; WP_012702044.1; NC_012560.1.
DR AlphaFoldDB; C1DQM8; -.
DR SMR; C1DQM8; -.
DR STRING; 322710.Avin_35150; -.
DR PRIDE; C1DQM8; -.
DR EnsemblBacteria; ACO79664; ACO79664; Avin_35150.
DR KEGG; avn:Avin_35150; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_6; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 304020at2; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.250.10; -; 1.
DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN 1..429
FT /note="Probable M18 family aminopeptidase 2"
FT /id="PRO_1000206330"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
SQ SEQUENCE 429 AA; 46936 MW; 30BE1C4BBDC1E3E6 CRC64;
MRTELNQGLI DFLKASPTPF HACASLAQRL ESAGYQRLDE REPWPTQSGG RYYVTRNDSS
LIAIQLGRRS PLEGGLRLVG AHTDSPCLRV KPQPELNRQG FWQLGVEVYG GALLAPWFDR
DLSLAGRVTF RRAGRVESQL IDFKQPIAVI PNLAIHLNRE ANQGWAINAQ NELPPILAQV
AGDERGDFRA LLAEQLQREH EINADVVLDF ELCFYDTQSA ALIGLNQDFI AGARLDNLLS
CHAGLQALLA AGDRESCVLV CTDHEEIGSC STCGADGPFL EQVLGRLLPD GDAFVRIMQQ
SLLVSADNAH GVHPNYADRH DANHGPKLNA GPVIKVNSNQ RYATNSETAG FFRHLCFDVE
VPVQSFVVRS DMGCGSTIGP ITASRLGMRT VDIGLPTFAM HSIRELAGSH DLTHLVKVLT
AFYSSPLLP