ID R9IWF3_9FIRM Unreviewed; 376 AA.
AC R9IWF3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=LLPSF_NHT_00031 family aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C806_01445 {ECO:0000313|EMBL:EOS26229.1};
OS Lachnospiraceae bacterium 3-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397288 {ECO:0000313|EMBL:EOS26229.1, ECO:0000313|Proteomes:UP000014188};
RN [1] {ECO:0000313|EMBL:EOS26229.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-1 {ECO:0000313|EMBL:EOS26229.1};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-1.";
RL Submitted (APR-2013) 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 DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:EOS26229.1}.
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DR EMBL; ASST01000007; EOS26229.1; -; Genomic_DNA.
DR AlphaFoldDB; R9IWF3; -.
DR STRING; 397288.C806_01445; -.
DR PATRIC; fig|397288.3.peg.1561; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_9; -.
DR Proteomes; UP000014188; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000014188}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 376 AA; 42299 MW; 8A7B45258337D42E CRC64;
MMKKILLATP TMHTEEQQYI QKAFETNWIS PLGPNVDEFE NKVAAYVGAS SSAALSSGTA
ALHLSVVLAG VKENDIVFVP SLTFAASVNP IRYEYATPVF IDSERDTWNM DAAALRKAFE
KYPHPKAVMA VHLYGTSANM DEICALCKEH NVPLIEDAAE SLGTTYKGKM TGTFGDYGIY
SFNGNKIITT SGGGILVAKQ EKDVDKARFL SRQARDPARY YQHSTIGYNY RMSNVVAGIG
CGQMQHIEEH IQKKQEIYKA YKEAFSDIEE IEMNPLNREG IDNNWLSCMT ISSDSDVTPT
QVMDALEAEN IETRPIWKPM HLQPVFEEYD FIQVEDGISV SEDIFNRGLC LPSDIKNTKE
DMERIIKIVR KQFRQQ
//
