ID I0A2L7_FERFK Unreviewed; 367 AA.
AC I0A2L7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:AFH43224.1};
GN OrderedLocusNames=FFONT_1236 {ECO:0000313|EMBL:AFH43224.1};
OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC Fervidicoccus.
OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH43224.1, ECO:0000313|Proteomes:UP000007391};
RN [1] {ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Fervidicoccus fontis complete genome analysis confirms its distinct
RT phylogenetic position and predicts its environmental function.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH43224.1, ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "Analysis of the complete genome of Fervidococcus fontis confirms the
RT distinct phylogenetic position of the order Fervidicoccales and suggests
RT its environmental function.";
RL Extremophiles 18:295-309(2014).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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; CP003423; AFH43224.1; -; Genomic_DNA.
DR AlphaFoldDB; I0A2L7; -.
DR STRING; 1163730.FFONT_1236; -.
DR KEGG; ffo:FFONT_1236; -.
DR eggNOG; arCOG00118; Archaea.
DR HOGENOM; CLU_033332_7_2_2; -.
DR InParanoid; I0A2L7; -.
DR OrthoDB; 10355at2157; -.
DR Proteomes; UP000007391; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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:AFH43224.1};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000007391};
KW Transferase {ECO:0000313|EMBL:AFH43224.1}.
SQ SEQUENCE 367 AA; 40759 MW; 010A487F48078342 CRC64;
MEVKIPISKP IIEQDEIDAV IEVLKSGMLT RGKNTELFEK EFASYIGTKY AVTVTNGTVA
LEAALKALGV GEGDEVIVPD FTFIATANAV VNVGGRPVFA DIDERTYCID PESVNEKITN
RTRAIIPVHL FGHMADMNSI NEIAIDNKLV VLEDSAQAHG AEMNGVKAGS IGHASAFSFY
ATKNMMTGEG GMVTTNLDAV YEFLVKWKKH GEAKRYLSDT LGTNLSMTEM QAAIGRVQLK
KLDRFNEIRR QNAAYFTKEL SKVKEIKTPV ELPGYKHVYH QYVIRVPAED RDKLIEHLNK
LGIGTAIHYP YPLHIQPIYK AMGYPEKQNP VSLEVSKEVL SIPVHPLLSK SDLEYIVKGI
LSYFNQA
//
