ID E8LFB7_9FIRM Unreviewed; 415 AA.
AC E8LFB7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:EFY04516.1};
GN ORFNames=HMPREF9443_01557 {ECO:0000313|EMBL:EFY04516.1};
OS Phascolarctobacterium succinatutens YIT 12067.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Phascolarctobacterium.
OX NCBI_TaxID=626939 {ECO:0000313|EMBL:EFY04516.1, ECO:0000313|Proteomes:UP000004923};
RN [1] {ECO:0000313|EMBL:EFY04516.1, ECO:0000313|Proteomes:UP000004923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12067 {ECO:0000313|EMBL:EFY04516.1,
RC ECO:0000313|Proteomes:UP000004923};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2011) 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}.
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:EFY04516.1}.
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DR EMBL; AEVN01000073; EFY04516.1; -; Genomic_DNA.
DR RefSeq; WP_009145910.1; NZ_GL830907.1.
DR AlphaFoldDB; E8LFB7; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_9; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000004923; Unassembled WGS sequence.
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 PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
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:EFY04516.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000004923};
KW Transferase {ECO:0000313|EMBL:EFY04516.1}.
SQ SEQUENCE 415 AA; 44701 MW; 0335A152E154EA25 CRC64;
MSNYVEETIG KYEKYINPAQ AKLFRFMGLA SIEGHAEGWT ITDSEGQEFI DCLGGYGMFA
LGHRHPKVVE AVEKELHAMP MCGKVLFNRP MADLAEALAE ITPGELQYSF FVNSGTESVE
GCLKVARLAT KRKKFVAAKN AFHGKTFGSL TATGRDMYRE PFKPLLDGFT HVEYGDAAAV
DAAVDEDTAA VILEPVQGEG GIIVPPAGYL REVKEICEKK GALLIADEVQ TGIGRTGEWF
GVNYDGVTPD MMACAKALGG GVMPIGAIIG TPRAWAGLIE APFLHTSTFG GNQLACAAGV
AAIKAIKEED MLRRGREAGA YLKAGLEAIA AEYPSVIKEV RGRGMMIGIE LTKEGAGGML
MSLMINQHII VAYTLNNPKV IRMEPPLIMP KEVIDHVLEA FRGAVKETAD VIEDL
//
