ID D2RRL5_HALTV Unreviewed; 451 AA.
AC D2RRL5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADB60575.1};
GN OrderedLocusNames=Htur_1690 {ECO:0000313|EMBL:ADB60575.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB60575.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB60575.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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 ---------------------------------------------------------------------------
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; CP001860; ADB60575.1; -; Genomic_DNA.
DR RefSeq; WP_012942871.1; NC_013743.1.
DR AlphaFoldDB; D2RRL5; -.
DR STRING; 543526.Htur_1690; -.
DR GeneID; 8742284; -.
DR KEGG; htu:Htur_1690; -.
DR eggNOG; arCOG00915; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR OrthoDB; 7184at2157; -.
DR Proteomes; UP000001903; Chromosome.
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; PTHR43206:SF2; 4-AMINOBUTYRATE AMINOTRANSFERASE GABT; 1.
DR PANTHER; PTHR43206; AMINOTRANSFERASE; 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:ADB60575.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADB60575.1}.
SQ SEQUENCE 451 AA; 49410 MW; 8559F9CE05FE10D1 CRC64;
MDRDTVEPQV GTIPDKRARQ WADYHHEFAA PSTYVYEFVW DATAEAVGPF CTDVDGNVLL
DFTSHVAAAP LGYNHPAVRE KLEEFDLVDP LKIAGQDFYV SGGGAPEDPD FPGPTQLMDR
LVAMTDQFDM DRVFLSNSGA EAVENAIKIC YAAGGHRAFT FDGAFHGRTL GALSLNRSKA
VHRRGYPEIP GVVSVPYPST DGEYERRWRT DGPGGNVVAD KLHPERGVID PDEVAYLILE
PIQGEGGYRV AHPEFARDLE ALRDRYDLNI VADEIQSGIG RTGELWAVDH LDLTPDVITA
GKGLRVGATI SRSDVFPAEK SRLSSTWGAG DIIASLQGAL TIDTIHEENL LANARERGRQ
LRERLEDAIA DGDAPGALEV RGRGLMLAVE FDTKERREAV LEAAFQRGLL TLGCGYKTLR
LLPPLSVTER EIDLGTELLL EAMADAESRL E
//
