ID   A0A136KWF1_9CHLR        Unreviewed;       427 AA.
AC   A0A136KWF1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:KXK13690.1};
GN   ORFNames=UZ14_CFX002001542 {ECO:0000313|EMBL:KXK13690.1};
OS   Chloroflexi bacterium OLB14.
OC   Bacteria; Chloroflexota; Tepidiformia.
OX   NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK13690.1, ECO:0000313|Proteomes:UP000070321};
RN   [1] {ECO:0000313|EMBL:KXK13690.1, ECO:0000313|Proteomes:UP000070321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB14 {ECO:0000313|EMBL:KXK13690.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK13690.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMZR01000038; KXK13690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KWF1; -.
DR   STRING; 1617415.UZ14_CFX002001542; -.
DR   Proteomes; UP000070321; 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:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:KXK13690.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KXK13690.1}.
SQ   SEQUENCE   427 AA;  46725 MW;  92FAA27BA8DFA12F CRC64;
     MTNQLYQDNF PHMTPAWSRI FNFVAERAEG SYIYTDDGKK LLDFTSGIGV TNTGHCHPQV
     VEAVRQQAGL FLHAQINLVI HKPMLQLIEE LRKVVPAPID SFYFANSGAE ALENAIKIAK
     VATGRQNVIV FNGSFHGRTH ATMALTTSKT IYRAGFAPLP ASIYVSPFPY AFNLGMSEEE
     ASAYALNQLE YLLASQTAPK ETAAILIETI LGEGGYIAPP KSFMKGLREI CDKHGIMLIL
     DEVQSGFGRT GKWFAFEHYD ILPDIMTVAK GIASGLPLSG VFSRTDIMRK LDTGSIGGTY
     GGNAIACAAG VATIRAMREE KMIENAAEKG IQLMTGLRKL QEEYPQIGDV RGKGLMVGTE
     FIVDGKQAKA KQLVKDVIHS AEEKGLLLLS CGTYDNTLRW IPPLNVTTEQ INDGLKIFAD
     SLKEVIK
//