ID A0A0J7XNC5_9SPHN Unreviewed; 416 AA.
AC A0A0J7XNC5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Aminotransferase V {ECO:0000313|EMBL:KMS53167.1};
GN ORFNames=V473_19485 {ECO:0000313|EMBL:KMS53167.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS53167.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS53167.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS53167.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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:KMS53167.1}.
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DR EMBL; JACT01000005; KMS53167.1; -; Genomic_DNA.
DR RefSeq; WP_066608106.1; NZ_KQ130436.1.
DR AlphaFoldDB; A0A0J7XNC5; -.
DR STRING; 1420583.V473_19485; -.
DR PATRIC; fig|1420583.3.peg.3697; -.
DR Proteomes; UP000052232; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KMS53167.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000052232};
KW Transferase {ECO:0000313|EMBL:KMS53167.1}.
FT DOMAIN 50..357
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 416 AA; 44257 MW; 7F11EF7689777BA5 CRC64;
MPPLDDLLAS GFFGEIDPPQ RLLMGPGPVN AHPRVLRAMS ADLLGQFDPE MTGYMNQVMA
LYRPIFGTQN PWTMLIDGTA RAGIEAALVS LVAPGDTVLV VNFGRFGLLL TEILGRIGAR
IETVEAPWGE VVPMDAIAAA IERVQPSVVA TIHGDTSTTM AQPLDGLGAL CAAAGALLYV
DATATIGGME LAADRWGADI VTGGLQKCLG GPSGSAPITI SDPAAALIQG RKHVEAGIRR
DDISDGAGPR IGSNYFDLAM IMDYWSDKRL NHHTEATSML YAARECARIM LGEGLEARYA
RHEAAGRAMT AGLRAMGLTI FGDDAHRMTN VTGVFIPQGV DGERVRTMMR NAFEIEIGTA
FGPLQGRIWR IGAMGYNAMQ HKVLITLGAL EACLRQEGFA LPAGEAVRVA MEAWDA
//
