ID A0A428K1D6_9RHOB Unreviewed; 427 AA.
AC A0A428K1D6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Aminotransferase class III-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RSK40207.1};
GN ORFNames=EJA01_00565 {ECO:0000313|EMBL:RSK40207.1};
OS Rhodovulum robiginosum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=68292 {ECO:0000313|EMBL:RSK40207.1, ECO:0000313|Proteomes:UP000275159};
RN [1] {ECO:0000313|EMBL:RSK40207.1, ECO:0000313|Proteomes:UP000275159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12329 {ECO:0000313|EMBL:RSK40207.1,
RC ECO:0000313|Proteomes:UP000275159};
RA Gupta D., Guzman M.S., Bose A.;
RT "Draft genome sequence of a marine photoferrotrophic bacterium, Rhodovulum
RT robiginosum.";
RL Submitted (DEC-2018) 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:RSK40207.1}.
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DR EMBL; RWGU01000029; RSK40207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428K1D6; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000275159; 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; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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:RSK40207.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000275159};
KW Transferase {ECO:0000313|EMBL:RSK40207.1}.
SQ SEQUENCE 427 AA; 45772 MW; 46DC9641D4F8DE42 CRC64;
MTGKAALLAR RERLMGPNVP TFYDDPVHIV RGHGVWLWDI EGRIYLDAYN NVPHVGHCHP
WVAAAIAAEV GTLNTHTRYL HEAVLDYIER LTATMGHDLS QAIMVCTGSE ANDIALRVAQ
AATGKTGIIA TDNTYHGNTS AVSQLSTRRP PIGGYPSHVR LVPAPDSLRP LGGSLAAQPA
AFAENVARAV DELQAAGHGL AGFMFCPFFA NEGFPVTAPG FLDPAVEVIR RAGGLLLADE
VQPGFGRLGS HFWGYEWLGV APDVVTLGKP MANGHPVAAL VTRPDLMAAF RTAFGYFNTF
GGNPVSAAAA LATLEALEAD GLQDNARTTG AYAKERLRAL DHPFLAEVRG QGLFFGAEFV
TDEAMTPATD FTARLVEAVR AKGVLMGRIG RAMNILKIRP PMPFSRDNTD FLIDRLAEAL
AETEITP
//
