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Database: UniProt
Entry: A0A257GHI4_9RHOB
LinkDB: A0A257GHI4_9RHOB
Original site: A0A257GHI4_9RHOB 
ID   A0A257GHI4_9RHOB        Unreviewed;       427 AA.
AC   A0A257GHI4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OYU37866.1};
GN   ORFNames=CFE33_18655 {ECO:0000313|EMBL:OYU37866.1};
OS   Pseudorhodobacter sp. PARRP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudorhodobacter.
OX   NCBI_TaxID=2015560 {ECO:0000313|EMBL:OYU37866.1, ECO:0000313|Proteomes:UP000215760};
RN   [1] {ECO:0000313|EMBL:OYU37866.1, ECO:0000313|Proteomes:UP000215760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PARRP1 {ECO:0000313|EMBL:OYU37866.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU37866.1}.
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DR   EMBL; NKIU01000011; OYU37866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257GHI4; -.
DR   Proteomes; UP000215760; 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:OYU37866.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215760};
KW   Transferase {ECO:0000313|EMBL:OYU37866.1}.
SQ   SEQUENCE   427 AA;  45498 MW;  6C37FCD53B40E473 CRC64;
     MTTNAQMIER RTRLLGPNVR LFYDDPLHLV KGAGTYVWDA DGRKYLDCYN NVPHVGHCHP
     AVIEAITRQA SQLNTHTRYL HENILDFVER LTGTFGPQIT SAIMVCTGSE ANDVALRMAQ
     AITGKTGIIA TDKTYHGNTT AVSHLSTRMP PIGGHGGHVR HIPAPDSYRP LGGVPGAAHA
     QALADAVEEA CQSLIASGHG VSGMILCPFF VNEGFPDLPS GFLDLAIAVV RKHGGVIIAD
     EVQPGFGRIG THFWGHLKAG FAPDIVTMGK PMGNGHPVAC VATSFEIISA FRKAFRYFNT
     FGGNPVSCAA ANAVLDVLGS EDLPAKAVVT GEHLRAGFRK LAEKHDIIGD VRGSGLANGL
     ELVLDRTTKA PATEIATKII NDLRQRGLLM GTNGINYNVL KIRPPMAFGI AEADQVIAAI
     DDVLGAL
//
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