BPT_AROAE
ID BPT_AROAE Reviewed; 246 AA.
AC Q5P1A8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Aspartate/glutamate leucyltransferase {ECO:0000255|HAMAP-Rule:MF_00689};
DE EC=2.3.2.29 {ECO:0000255|HAMAP-Rule:MF_00689};
GN Name=bpt {ECO:0000255|HAMAP-Rule:MF_00689}; OrderedLocusNames=AZOSEA27810;
GN ORFNames=ebA4890;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
CC -!- FUNCTION: Functions in the N-end rule pathway of protein degradation
CC where it conjugates Leu from its aminoacyl-tRNA to the N-termini of
CC proteins containing an N-terminal aspartate or glutamate.
CC {ECO:0000255|HAMAP-Rule:MF_00689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) +
CC N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu);
CC Xref=Rhea:RHEA:50412, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC Rhea:RHEA-COMP:12664, Rhea:RHEA-COMP:12668, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64721, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC ChEBI:CHEBI:133041; EC=2.3.2.29; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00689};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) +
CC N-terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu);
CC Xref=Rhea:RHEA:50420, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC Rhea:RHEA-COMP:12669, Rhea:RHEA-COMP:12674, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64720, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC ChEBI:CHEBI:133042; EC=2.3.2.29; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00689};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00689}.
CC -!- SIMILARITY: Belongs to the R-transferase family. Bpt subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00689}.
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DR EMBL; CR555306; CAI08906.1; -; Genomic_DNA.
DR RefSeq; WP_011238589.1; NC_006513.1.
DR AlphaFoldDB; Q5P1A8; -.
DR SMR; Q5P1A8; -.
DR STRING; 76114.ebA4890; -.
DR PRIDE; Q5P1A8; -.
DR EnsemblBacteria; CAI08906; CAI08906; ebA4890.
DR KEGG; eba:ebA4890; -.
DR eggNOG; COG2935; Bacteria.
DR HOGENOM; CLU_077607_0_0_4; -.
DR OMA; MVEDSHV; -.
DR OrthoDB; 1675133at2; -.
DR Proteomes; UP000006552; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004057; F:arginyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008914; F:leucyltransferase activity; IEA:InterPro.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:InterPro.
DR HAMAP; MF_00689; Bpt; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR017138; Asp_Glu_LeuTrfase.
DR InterPro; IPR030700; N-end_Aminoacyl_Trfase.
DR InterPro; IPR007472; N-end_Aminoacyl_Trfase_C.
DR InterPro; IPR007471; N-end_Aminoacyl_Trfase_N.
DR PANTHER; PTHR21367; PTHR21367; 2.
DR Pfam; PF04377; ATE_C; 1.
DR Pfam; PF04376; ATE_N; 1.
DR PIRSF; PIRSF037208; ATE_pro_prd; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..246
FT /note="Aspartate/glutamate leucyltransferase"
FT /id="PRO_0000263170"
SQ SEQUENCE 246 AA; 29226 MW; 0F37F1806BF567D0 CRC64;
MQKDYPYALI QFYATAPYTC SYLSDRVARS QVATPGHLID TPVYSELVRN GFRRSGMFTY
RPYCDHCRAC VPVRIPVKRF EPDRSQRRAW KMHHELRANE QPLAYSEEHY ALYQRYQGSR
HAGGGMDQDN REQYAHFLLQ SHVDTRLVEF REGDVLRMVS VIDRLSDGLS SVYTFYDPDQ
THASYGTYGI LWQIEVCRRL KLPYLYLGYW IKESRKMTYK VRFHPLEGRL RGEWRDIDPL
RDRASE