ID I8R5E1_9THEO Unreviewed; 372 AA.
AC I8R5E1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative PLP-dependent enzyme possibly involved in cell wall biogenesis {ECO:0000313|EMBL:EIW00675.1};
GN ORFNames=ThesiDRAFT1_1792 {ECO:0000313|EMBL:EIW00675.1};
OS Thermoanaerobacter siderophilus SR4.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=880478 {ECO:0000313|EMBL:EIW00675.1};
RN [1] {ECO:0000313|EMBL:EIW00675.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR4 {ECO:0000313|EMBL:EIW00675.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Hemme C., Woyke T.;
RT "Improved High-Quality Draft sequence of Thermoanaerobacter siderophilus
RT SR4.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CM001486; EIW00675.1; -; Genomic_DNA.
DR RefSeq; WP_006570123.1; NZ_CM001486.1.
DR AlphaFoldDB; I8R5E1; -.
DR PATRIC; fig|880478.3.peg.175; -.
DR HOGENOM; CLU_033332_7_2_9; -.
DR Proteomes; UP000005110; Chromosome.
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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 372 AA; 42146 MW; D55A59C8E6C51464 CRC64;
MKVPLSRPDI TQKEINAVVE VLKSDILSIG PKIEEFERKI ADYVGKKYAI AVNSGTSALH
LIVRSLGIKG GDEVITTPFT FIASVNCFLF ERAKPVFVDI NPDTLNMDIS KIEEKITEKT
KAILTVDVFG QPMDMERVNK IAKKYGLKVI EDSCEALGSE YKGIKAGTLC DAGAFAFYPN
KQITTAEGGV IVTDNEEIAQ LSRSMRSQGR PITGLWLEHE RLGFNYRLSE LHAALGIVQL
ERIEEIIKRR SEIAEKYNER LKDVKGVKIP YIAPEVNKMS WFVYVIRVDE NIDRDKVMQY
LIDNDIGCRP YFTPVHLQSY IKKLTGHKEG DFPITEKVAR STIALPFFNK ITDEQIDYVV
DKLKEAIKIY SR
//