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Database: UniProt
Entry: Q30S51_SULDN
LinkDB: Q30S51_SULDN
Original site: Q30S51_SULDN 
ID   Q30S51_SULDN            Unreviewed;       363 AA.
AC   Q30S51;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ABB44180.1};
GN   OrderedLocusNames=Suden_0902 {ECO:0000313|EMBL:ABB44180.1};
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB44180.1, ECO:0000313|Proteomes:UP000002714};
RN   [1] {ECO:0000313|EMBL:ABB44180.1, ECO:0000313|Proteomes:UP000002714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP000153; ABB44180.1; -; Genomic_DNA.
DR   RefSeq; WP_011372532.1; NC_007575.1.
DR   AlphaFoldDB; Q30S51; -.
DR   STRING; 326298.Suden_0902; -.
DR   KEGG; tdn:Suden_0902; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_6_1_7; -.
DR   OrthoDB; 9766188at2; -.
DR   Proteomes; UP000002714; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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:ABB44180.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002714};
KW   Transferase {ECO:0000313|EMBL:ABB44180.1}.
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         186
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   363 AA;  39889 MW;  49C764A69228E3BA CRC64;
     MKINFIDLQA QYKKYETEIN SEVMEVFNSA QFIGGEKLDK LEKNLAAYTG AKHAIGCSSG
     TDALLLALMA LDIGDGDEII TTPFTFIATA EVIALLGAKS VFIDIDEESY NIDPSKIEAA
     ITDRTKAIIP VSLYGQCADM DKINDIAKRH NLIVIEDACQ SFGASYFDKK SCNLSTIACT
     SFFPSKPLGA YGDGGAIFTS DDELALKMRM LLNHGQNERY KHKYIGINGR LDAIQAAILN
     VKLKHFEEEA NLRDEIGSRY SDLLEDADVI TPKISEGNIS VYAQYSIRVK DREAMVAKLS
     ALGVPTAVHY PVPLHLQEAF KHLGYGEGDF PISELISTQI MSLPMSAFLS ETEQDFVVQA
     IKG
//
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