ID A0LEL9_SYNFM Unreviewed; 372 AA.
AC A0LEL9;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Peptidase M24 {ECO:0000313|EMBL:ABK15871.1};
GN OrderedLocusNames=Sfum_0169 {ECO:0000313|EMBL:ABK15871.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15871.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK15871.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000478; ABK15871.1; -; Genomic_DNA.
DR RefSeq; WP_011697044.1; NC_008554.1.
DR AlphaFoldDB; A0LEL9; -.
DR STRING; 335543.Sfum_0169; -.
DR KEGG; sfu:Sfum_0169; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_2_7; -.
DR InParanoid; A0LEL9; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProt.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT DOMAIN 9..145
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 153..355
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 372 AA; 41582 MW; 7E562E016237B2E8 CRC64;
MSESMFDVRL ERFRKLCGEE GLDAFLVANP ENRYYLSGYE ADDMHLTESS GFLLITPDRR
YLLTDPRYEE AARKEAPGFA VRIYTQGLSQ VLAELLPEIR PERLGAESSY LTWSRYKDVE
EQLRKANPSA VVLGFEGLVE RLRVIKEPME IEWIKASLRL TEDALVAVWN ELAPGRKEKD
IAWRIERYIR EGGGEAVSFP PIVAAGPNGA LPHAVPGERR IAKGDSLILD LGSKLRHYCS
DMTRTWIAGN PEPKLAEIYR VVREAQLAAQ DQLRAGIDSV EVDRVARDLI AKAGYGEYFG
HGLGHGVGLA VHEGPSLRRF HGTILEENMV VTVEPGIYLP GYGGVRLENM VRITATGCEV
LNTRDLFLEQ AG
//
