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Database: UniProt
Entry: V9VRV5_9RHOB
LinkDB: V9VRV5_9RHOB
Original site: V9VRV5_9RHOB 
ID   V9VRV5_9RHOB            Unreviewed;       401 AA.
AC   V9VRV5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:AHD00424.1};
GN   ORFNames=METH_06505 {ECO:0000313|EMBL:AHD00424.1};
OS   Leisingera methylohalidivorans DSM 14336.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD00424.1, ECO:0000313|Proteomes:UP000018780};
RN   [1] {ECO:0000313|EMBL:AHD00424.1, ECO:0000313|Proteomes:UP000018780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD00424.1,
RC   ECO:0000313|Proteomes:UP000018780};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP006773; AHD00424.1; -; Genomic_DNA.
DR   RefSeq; WP_024089579.1; NC_023135.1.
DR   AlphaFoldDB; V9VRV5; -.
DR   STRING; 999552.METH_06505; -.
DR   KEGG; lmd:METH_06505; -.
DR   PATRIC; fig|999552.6.peg.1316; -.
DR   HOGENOM; CLU_033332_7_2_5; -.
DR   OrthoDB; 9768668at2; -.
DR   Proteomes; UP000018780; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AHD00424.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:AHD00424.1}.
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         187
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   401 AA;  43481 MW;  54D33C0139DE93CB CRC64;
     MALPPNVHDA EPIPAAAREA IEALMQSGDL FRYTAPENAP VTLLEQEYAD LLGSKYALAV
     SSCSAALFLS LKALSLPRDA RVLIPAFTFA AVPSSVVHAD CVPVLCEVGE NYRIDMADFE
     AKLDSVQAVI ISHMRGHTSD MDAIMALCDA RGIPVVEDAA HSLGTTWNGR NIGTIGKVGC
     FSFQSYKMVN GGEGGILITD DAGLIARAVI MSGAYEHNWK KHKGPRGENA PDLEQAFAKW
     QNQLPLYNLR MSNLSAAVIR PQLPELARRV RDGLANHDYV AARLNASPYF DVPAPLAPER
     RAPDSIQFNL AGLSEAQTRA FASTAEAKGV KVQVFGLSSD NARAFWNWQF LRDQPELPQT
     RAMLMKACDV RLPVRLTRAE LDVIADILLA AAKETMARAA A
//
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