ID E6U9H3_ETHHY Unreviewed; 450 AA.
AC E6U9H3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADU26164.1};
GN OrderedLocusNames=Ethha_0587 {ECO:0000313|EMBL:ADU26164.1};
OS Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 /
OS YUAN-3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ethanoligenens.
OX NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU26164.1, ECO:0000313|Proteomes:UP000001551};
RN [1] {ECO:0000313|EMBL:ADU26164.1, ECO:0000313|Proteomes:UP000001551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3
RC {ECO:0000313|Proteomes:UP000001551};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A.,
RA Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.;
RT "Complete sequence of Ethanoligenens harbinense YUAN-3.";
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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP002400; ADU26164.1; -; Genomic_DNA.
DR RefSeq; WP_013484536.1; NZ_CP025286.1.
DR AlphaFoldDB; E6U9H3; -.
DR STRING; 663278.Ethha_0587; -.
DR KEGG; eha:Ethha_0587; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_9; -.
DR Proteomes; UP000001551; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 1.
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; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF112; PUTRESCINE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ADU26164.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001551};
KW Transferase {ECO:0000313|EMBL:ADU26164.1}.
SQ SEQUENCE 450 AA; 49276 MW; E302CF8C46287B64 CRC64;
MSYADVSKDL ERVIGYIHAD KLTDEEKETM TRETLHYFDE YVSPGWLKYR KSVSTNSAVL
EWTDRDSVLD GMNGEEFIDC LGGFGIYTCG HRNPEILDTV KAQLDHQALH SQELLDPLRG
YLAKAVADIT PGDLGKCFFT NGGAEAVEMS LKLARIATGG RWFVSTVSAF HGKSMGAISV
GGKNTFRIPY TPMVQQVVHV EYGNAEDTRK AVRNLQAVGE KVAAVIVEPI QGEAGVIVPP
EGYLKELRAV CDECGVALIF DEIQTGMGRT GTMWRCEVEN VTPDILIFGK AFGGGIMPIT
GLICRPPMWT QQLIDNPWLL GSPTFGGNPV CCSAALATIK FMIDHDIPGQ AKRKGAVLKA
GLQKLKEKYP AVIVDVRGEG LMLAVEFEKS EIGYSIAKGM FARGVLTAGT LNNSKTVRFE
PPAVITEEQI EKVLARMDEA LAETEREFAR
//
