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Database: UniProt
Entry: G9XQ88_DESHA
LinkDB: G9XQ88_DESHA
Original site: G9XQ88_DESHA 
ID   G9XQ88_DESHA            Unreviewed;       389 AA.
AC   G9XQ88;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase family protein {ECO:0000313|EMBL:EHL06048.1};
GN   ORFNames=HMPREF0322_03134 {ECO:0000313|EMBL:EHL06048.1};
OS   Desulfitobacterium hafniense DP7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=537010 {ECO:0000313|EMBL:EHL06048.1, ECO:0000313|Proteomes:UP000004416};
RN   [1] {ECO:0000313|EMBL:EHL06048.1, ECO:0000313|Proteomes:UP000004416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP7 {ECO:0000313|EMBL:EHL06048.1,
RC   ECO:0000313|Proteomes:UP000004416};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHL06048.1}.
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DR   EMBL; AFZX01000086; EHL06048.1; -; Genomic_DNA.
DR   RefSeq; WP_005813492.1; NZ_JH414480.1.
DR   AlphaFoldDB; G9XQ88; -.
DR   PATRIC; fig|537010.4.peg.2931; -.
DR   HOGENOM; CLU_033332_0_3_9; -.
DR   Proteomes; UP000004416; 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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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:EHL06048.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:EHL06048.1}.
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         187
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   389 AA;  43754 MW;  4C2D63C4820719E2 CRC64;
     MNNRVIPFSP PDITDLEINA VVEVLKSGWI TSGPKVHLLE EKLQEYCQAD HAVALASNSQ
     GLDLILKVLN ISGEAEILTT PYTYVATANA ALHRGIKPTF IDLKKDSFFM DEEKLYDAIS
     DKTKVILTVD IGGVPMDYDV VKNILREKNR EDILLISDSA HSIGAAYKGA PVGTQFDFHV
     FSFHAVKNLT TAEGGAITFN GDRENLVQVF KYSSLNGQTK DALSKMKAGA WRYDILTDGL
     KCNMTDIGAA IGLVQLDRYD KILGQRKKLS HIYHSILSEK EWALLPLLEN DIMESSYHLY
     PLRIQGFTEE QRDRVIQELA EMGIATNVHY IPIPMFTYYK ELGYDIQDYP NTYAQYANEI
     TLPLYSILTS ADCEYVAENV IKAVEKHRK
//
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