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Database: UniProt
Entry: A0A1G1TEW1_9BACT
LinkDB: A0A1G1TEW1_9BACT
Original site: A0A1G1TEW1_9BACT 
ID   A0A1G1TEW1_9BACT        Unreviewed;       450 AA.
AC   A0A1G1TEW1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Aminotransferase class III {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BEN47_07130 {ECO:0000313|EMBL:OGX89408.1};
OS   Hymenobacter lapidarius.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1908237 {ECO:0000313|EMBL:OGX89408.1, ECO:0000313|Proteomes:UP000176294};
RN   [1] {ECO:0000313|EMBL:OGX89408.1, ECO:0000313|Proteomes:UP000176294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8643 {ECO:0000313|EMBL:OGX89408.1,
RC   ECO:0000313|Proteomes:UP000176294};
RA   Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E., Vrbovska V.,
RA   Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT   "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT   Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       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:OGX89408.1}.
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DR   EMBL; MDZB01000022; OGX89408.1; -; Genomic_DNA.
DR   RefSeq; WP_070724315.1; NZ_MDZB01000022.1.
DR   AlphaFoldDB; A0A1G1TEW1; -.
DR   STRING; 1908237.BEN47_07130; -.
DR   OrthoDB; 9762089at2; -.
DR   Proteomes; UP000176294; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   450 AA;  49699 MW;  E8974F004A58E463 CRC64;
     METAYATDPT QILHDNLDHT LFSWSKQTGL NPINAERAEG VYVYDRDGKR YIDFSSQLMN
     VNIGHGDQRV TEAVAAQMRE LSYVYPGMIT KARGDLGRRL AEITAPNLTK AFFTLGGAEA
     IENAIKLARV YTGRHKIVTL YLSFHGASYG AMSAGGDPRK FAVDSQAMPG VVHVENPYSY
     RCPWYSDSPE QCAQRAADAM ERIIGYENPG SVAAIIMEGE SGTSGCIKYP PGYWTRVREI
     CDKHGILLIA DEVMSGFGRT GKWFGSDHHG VKVDVMCMAK GITAGYLPLG AVMVDEKIAK
     SFDDKPLPLG LTYSAHPVSC AAAVAVLDIY ESDNLLENTV EMGEYMDQQV AQLMRHHPSI
     GDWRNTGLFG CLELVKNRAT KEPMAPWNAN NDQMAIMNQV AAKIRELGMY TFVRWSYIFI
     CPPLTITKEE IDEGLAIISE AISIADKHVN
//
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