ID A0A136N1D1_9BACT Unreviewed; 767 AA.
AC A0A136N1D1;
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=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KXK39856.1};
GN ORFNames=UZ09_BCD002000762 {ECO:0000313|EMBL:KXK39856.1};
OS Bacteroidetes bacterium OLB9.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK39856.1, ECO:0000313|Proteomes:UP000070267};
RN [1] {ECO:0000313|EMBL:KXK39856.1, ECO:0000313|Proteomes:UP000070267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK39856.1};
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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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:KXK39856.1}.
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DR EMBL; LNBW01000022; KXK39856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136N1D1; -.
DR STRING; 1617420.UZ09_BCD002000762; -.
DR PATRIC; fig|1617420.3.peg.813; -.
DR Proteomes; UP000070267; 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; 3.90.1200.10; -; 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; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KXK39856.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:KXK39856.1}.
FT DOMAIN 26..240
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 767 AA; 85784 MW; 7B866C32C6DECAF1 CRC64;
MISQDIHRVQ KIAREAYGII AEAKPLSGYE DINFLLETQQ GEKFIFKIST ASSCLDFLQA
QAEVMKLLSI SNMKGHFPVH IPNLNDELIT ISSSGGKVQY IRVLSWIEGD FWVNWLDKDR
KLYESLGAFL GEMDSILNGL YISAAERYLS WDICRASDAV EHLQNIHDPE KRRIAGYFLL
QFHTEVFPKL NHLRKAIIHN DANDYNVLVS DDKVVGLIDF GDMVWSALIN NLAIACTYAM
LDTNDPIEKA SWVIGAYHRV YPLQLQEIDL LYYLIASRLS ISVTQSATQM QKKSNNAHHF
LTDTQAWDLL QKLICTNPIK AADTFRKACD FAPLINENED YVALLSDRKK HIGRNLSISY
QQPLKIVKGA LQYLYDDKGR TYIDCVNNVS HVGHCHPDIV RTMQHQIAVL NTNTRYLSDL
MVSYAKELTQ LLPEKLNVCY FVNSGSEAND LAIRMARQYT GRKDIVVLDH AYHGTSTLAI
EMSPYKFDGQ GGSGQKPYIH KALSPDLYRG CFQSDDQNAG EKYAAQILEL LCQMTADDKP
IAAFICETLL GVGGQIPLPN GYLKKVYEYV HQYGGLCIAD EVQVGFGRVG SCFWGFELQE
VEPDIVVLGK PIGNGHPLAA VVVTDEIADA FNNGMEYFNT FGGNPVSMAT GSAVLKVLKN
ENLQAHALRT GNLLLSGLRQ LQNKYPIIGD VRGHGLFIGV EMVGDRITKT PAVEELNVVV
EAMKERGFLL STDGPLHNVL KIKPPLTFSE QNAKDLVRHL GEVLDSI
//
