ID R5PBD1_9BACT Unreviewed; 469 AA.
AC R5PBD1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:CCZ13850.1};
GN ORFNames=BN465_00338 {ECO:0000313|EMBL:CCZ13850.1};
OS Prevotella sp. CAG:1092.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ13850.1, ECO:0000313|Proteomes:UP000017987};
RN [1] {ECO:0000313|EMBL:CCZ13850.1, ECO:0000313|Proteomes:UP000017987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCZ13850.1}.
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DR EMBL; CAZL010000503; CCZ13850.1; -; Genomic_DNA.
DR AlphaFoldDB; R5PBD1; -.
DR STRING; 1262919.BN465_00338; -.
DR Proteomes; UP000017987; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01087; Prolidase; 1.
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; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000017987}.
FT DOMAIN 4..137
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 469 AA; 53102 MW; CC01509B2EBC384F CRC64;
MNMFSKETYV SRRAELKKLV KSGIIILFGN NDSPANFPNN AYSPFRQDSS FLYYFGQKRD
GLVGIIDIDN DMETLIGDDI SVEDIVWYGS VDSVHDMAQQ VGVANTAPMK TLKTICNDAL
RQKRKIHFLP PYRFDIKLQV FDLLGIHPNQ QKESASMDLI KAVVKMRSAK EPQEIEELER
AAVIGYKMHT TAMRMCKPGA IEQNIAGYLK GIAHGYGAME SFATILSQHG EIMHGAPSMN
PLEDGRLLLV DAGAETINNY CSDNTRTMPV NGKFTQRQLE IYSIVEECHD YALKAARPGV
KYWDVHFGVC RLMTDRLKEL GLMKGDTDEA VAAGAHAMFL CHGLGHMMGM DVHDMENFDQ
INVGFDEETR PNLEQFGTNC LRMGRRLEEG FVVTDEPGIY FIPALIDDWR SKGLHKDFIN
YDMLETYKDF GGIRIEDDLL ITKDGCRFLG KDRIPYHPKD VEEFMANNK
//
