ID B8CYS7_HALOH Unreviewed; 391 AA.
AC B8CYS7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ACL70446.1};
GN OrderedLocusNames=Hore_16970 {ECO:0000313|EMBL:ACL70446.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL70446.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL70446.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP001098; ACL70446.1; -; Genomic_DNA.
DR RefSeq; WP_015923416.1; NC_011899.1.
DR AlphaFoldDB; B8CYS7; -.
DR STRING; 373903.Hore_16970; -.
DR KEGG; hor:Hore_16970; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_4_9; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000000719; 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; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:ACL70446.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000719};
KW Transferase {ECO:0000313|EMBL:ACL70446.1}.
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 391 AA; 44233 MW; BA1067A4AF6D97A3 CRC64;
MEDKLNIPLS VPNLSLDILD NLKECIETGW VSTGGRFIKE FEDKVAKYVR VEEAVGVQSG
TGALHLGYQL LGVKPGDEVI VPTVTFIATV NPITYLGAHP VFMDCDDTLN MDLDKLEEFL
DSHCEITDKG LLNKKSKRII KVLTVTHIFG NPIDMERVMK IAGRYRLKVL EDAAESLGSF
YISGKYKGKH TGTIGDLGVF SFNANKILTT GGGGMIVAKD KKLVNKARFL STQAKTDPLY
FKHDEIGYNY RLTNIAAALG TSQIDKIEDF VKIKKENYHL YKKEINNIEG LELLPFNEGT
RPNYWFYSLI VNSEKYGLNR DELLHKLNSV GIQTRPLWGL VSKQKPYKNY FAYKIEKARY
YVNNLINIPC STNLKKEQVL QVIDKLKGFK K
//
