ID   E5WE77_9BACI            Unreviewed;       241 AA.
AC   E5WE77;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Acetylornithine aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1013_00752 {ECO:0000313|EMBL:EFV78868.1};
OS   Bacillus sp. 2_A_57_CT2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV78868.1, ECO:0000313|Proteomes:UP000003283};
RN   [1] {ECO:0000313|EMBL:EFV78868.1, ECO:0000313|Proteomes:UP000003283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV78868.1,
RC   ECO:0000313|Proteomes:UP000003283};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EFV78868.1}.
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DR   EMBL; ACWD01000011; EFV78868.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5WE77; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_2_9; -.
DR   Proteomes; UP000003283; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003283}.
SQ   SEQUENCE   241 AA;  25832 MW;  D8CFB748996F8314 CRC64;
     MLETFKYVPF NDINALEEEI DAETAAVMLE IVQGEGGIHI GNQEFLTKTE QLCKEYGALL
     IVDEIQTGIG RTGKAFGFQH FDLTPDIVTA AKGLGSGLPI GAVIGKKALE EVFGPGSHGS
     TFGGNPISIA AAIATMKTIF DDDFLQGVQE KSAYLADKLA ESLEQIEAVK EIRYLGLMVG
     IELDIPLPSL LKELRANCLL ALPAGENVLR LLPPLTASKS EIDEAVQILQ STLKEFSKSA
     V
//