ID B6BKH0_SULGG Unreviewed; 374 AA.
AC B6BKH0; H1FV99;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:EHP29025.1};
GN ORFNames=SMGD1_0498 {ECO:0000313|EMBL:EHP29025.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP29025.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP29025.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP29025.1,
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 -!- 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}.
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:EHP29025.1}.
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DR EMBL; AFRZ01000001; EHP29025.1; -; Genomic_DNA.
DR RefSeq; WP_008337778.1; NZ_DS995288.1.
DR AlphaFoldDB; B6BKH0; -.
DR STRING; 929558.SMGD1_0498; -.
DR PATRIC; fig|929558.5.peg.496; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_4_7; -.
DR OrthoDB; 9766188at2; -.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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:EHP29025.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006431};
KW Transferase {ECO:0000313|EMBL:EHP29025.1}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 43070 MW; 04DA68818C6D718A CRC64;
MKTIPNIGPW IGDFEKETVN KAMSDWYENP YYYCELFEKE FAKYHDRKYA LMTPNCTSAI
HLLMLGLGIQ EGDEVIGPEC TWIASVAPAF YQKAKVVLCD IDETTWCLDP KSVEKNITNK
TKAIVSVNLF GNMANWNELL KISKKYNIPL IEDAAQSLGS TYKGIKSGKF GIGSVFSFHR
TKTLTTGEGG MLLIDDDKLY KKCKMFRDHG RNDNDPMYFN SEVGYKYMPN NISASLGYAQ
FQRLDELVSK KHWILQQYSK RLNVIDDITL NYEPEYVYNS AWITTIVLGR SIQIKKQDFI
DKLISKNIMA RPFFYPLSSI PALNKRGYIE EEHKLKNPMA YDLSSRTINL PSPLNITEEQ
IDYICNEIKT ILMK
//
