ID   S6GRH7_9GAMM            Unreviewed;       442 AA.
AC   S6GRH7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Aspartate aminotransferase family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=OFPI_20630 {ECO:0000313|EMBL:EPJ50206.1};
OS   Osedax symbiont Rs2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ50206.1, ECO:0000313|Proteomes:UP000014830};
RN   [1] {ECO:0000313|EMBL:EPJ50206.1, ECO:0000313|Proteomes:UP000014830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EPJ50206.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ASZI01000150; EPJ50206.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6GRH7; -.
DR   PATRIC; fig|1330035.3.peg.1970; -.
DR   Proteomes; UP000014830; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014830}.
SQ   SEQUENCE   442 AA;  48113 MW;  AD5EF373963D7B38 CRC64;
     MSAVFQRNCN AKMPIAVKGD GVYIIDQNGK RYLDGCGGAA GSSLGHSHPR VKAAITEQLD
     KIPFAHTGFF SSEPAEQLAQ FLIDKAPGDM GKIYFTSGGS EAVEAALKLA RQYFLERDQP
     QRQLFISREQ SYHGNTLGAL GVGGNAWRRE PFAVLMNDAN YISPCYAYRG QQPGETEFDY
     GQRVATELET KLQQLGPETV LAFIAEPVVG ATLGAVPSVP GYFKRVREIC DNAGILLILD
     EVMCGMGRTG SLFAYEQEAI VPDMVTMAKG LGAGYQPIGA LMVSSEIHNT VASGSGFFQH
     GHTYIGHATA CAASMAVQQV IEEEQLLANV QTQGKYLKQQ LQQCFAEHPH IGDIRGRGLF
     LGFELVAERA DKSPLPLDSQ IQHKIKAQLM ENGLMCYPGA GSVDGRRGHH ILLAPPFIVE
     QQHLDFLVET LAKSIKQVLN RI
//