ID B6BKJ5_SULGG Unreviewed; 375 AA.
AC B6BKJ5; H1FVC4;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:EHP29050.1};
GN ORFNames=SMGD1_0523 {ECO:0000313|EMBL:EHP29050.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP29050.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP29050.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP29050.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:EHP29050.1}.
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DR EMBL; AFRZ01000001; EHP29050.1; -; Genomic_DNA.
DR RefSeq; WP_008337932.1; NZ_DS995288.1.
DR AlphaFoldDB; B6BKJ5; -.
DR STRING; 929558.SMGD1_0523; -.
DR PATRIC; fig|929558.5.peg.521; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_7; -.
DR OrthoDB; 5342089at2; -.
DR Proteomes; UP000006431; Unassembled WGS sequence.
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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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:EHP29050.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000006431};
KW Transferase {ECO:0000313|EMBL:EHP29050.1}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 375 AA; 42663 MW; 0153568A564F2FC3 CRC64;
MDFIPYGKQF IDEADFKAVA EALASPLITT GPIAKEFEKR LCEYTGAKYS IVVSNGTAAL
HLASIALLSA DDKVLTTPNS FLATSNAILY ANAKPIFVDI EENGNINLDL CEEAIKKDPT
IKAIYAVAFS GNPVDQKKLK HIRDTYNVKI LEDCAHAIGS EYDGIKAGSC VNSDCTIFSF
HPVKHMTTGE GGAITTNNKD IYEKIMLLRN HGMERKHDIA PWYYEMTVLG FNYRITDIQC
ALGISQLDKL NENIVRRRIL AQRYDNVFKR HEFIKPLYTY DGNSSYHLYV VKIDFNKLKV
SKIGLFNKLK EYNFGVMVHY IPINKQPYYR ELGYGDEDTP NMNKYYEETI SLPMYYSLSD
AEQDYVIKSL FEILK
//
