ID   A0A081BMU5_9BACT        Unreviewed;       534 AA.
AC   A0A081BMU5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:GAK51711.1};
GN   ORFNames=U14_02956 {ECO:0000313|EMBL:GAK51711.1};
OS   Candidatus Moduliflexus flocculans.
OC   Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC   Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX   NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK51711.1};
RN   [1] {ECO:0000313|EMBL:GAK51711.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA   Hugenholtz P.;
RT   "First genomic representation of candidate bacterial phylum KSB3 points to
RT   enhanced environmental sensing as a trigger of wastewater bulking.";
RL   PeerJ 3:e740-e740(2015).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; DF820457; GAK51711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081BMU5; -.
DR   STRING; 1499966.U14_02956; -.
DR   HOGENOM; CLU_033332_5_0_0; -.
DR   Proteomes; UP000030700; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 2.30.30.110; -; 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; IPR003477; PemK-like.
DR   InterPro; IPR011067; Plasmid_toxin/cell-grow_inhib.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   Pfam; PF02452; PemK_toxin; 1.
DR   SUPFAM; SSF50118; Cell growth inhibitor/plasmid maintenance toxic component; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:GAK51711.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW   Transferase {ECO:0000313|EMBL:GAK51711.1}.
SQ   SEQUENCE   534 AA;  60143 MW;  9355C4EFC53CB620 CRC64;
     MLSKIHVGEI YKVSFPFTDT SGCKGRPALV LSEPDIQGDV QVAFITTTKP TDGIRYIHLE
     TSHFDGEALP FPSYLNFSHS IRVPSSVILK PLARLTKKTM AEIFRRSICE QIPAFYEFAH
     APQPFRPGID PVPHGGRVFD AEEIESLVEA ALDFWLTTGQ YAAQFEQDFA KFLGMRYALL
     CNSGSSANLL ALSSLTSPKL KERQLRPGDE VITVAAGFPT TLNPILQNNL VPVLLDIELP
     TYNIDIQYLE EAIHPHTKAI LLAHTLGNPF PIDAVIDVAR RHNLWIIEDN CDALGSTYKG
     RLTGTFGDLA TFSFYPAHHI TMGEGGCVLT NAEVLRTLVA SFRDWGRDCW CSPGHDNTCA
     RRFEWKLGTL PQGYDHKYIF SHIGYNLKLT DMQAAIGVAQ LRKLPEFIEA RRRNWQHLFD
     GLHALEEFFV LPCPAPESQP SWFGFPLTVR TTAPFTRQRI IRFLEQQNIS TRLLFGGNLL
     RHPAYQDIPH RIVGTLTNTD VIMNQTFWIG VYPGLTEVML NYVIDNIRAF IKAL
//