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Database: UniProt
Entry: E1QEP5_DESB2
LinkDB: E1QEP5_DESB2
Original site: E1QEP5_DESB2 
ID   E1QEP5_DESB2            Unreviewed;       398 AA.
AC   E1QEP5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:ADK84031.1};
GN   OrderedLocusNames=Deba_0659 {ECO:0000313|EMBL:ADK84031.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK84031.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK84031.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP002085; ADK84031.1; -; Genomic_DNA.
DR   RefSeq; WP_013257486.1; NC_014365.1.
DR   AlphaFoldDB; E1QEP5; -.
DR   STRING; 644282.Deba_0659; -.
DR   KEGG; dbr:Deba_0659; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_7_2_7; -.
DR   OrthoDB; 9771070at2; -.
DR   Proteomes; UP000009047; 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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ADK84031.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW   Transferase {ECO:0000313|EMBL:ADK84031.1}.
SQ   SEQUENCE   398 AA;  43312 MW;  478EF65DB3B4F76E CRC64;
     MPGFEWLGRE EKEAVVDVMD RGVLFRYEFA EKRGDAWRVR QFEEAFAAYA GAKHALAVTS
     GSAALKVALC ALGVGPGDEV ITQGFTFVAT WEAILDCGAE PVFCEIDDTL CMDPADLEKK
     ITPRTRCIVP VHMMGAPADI GRIKAVADAH GVPVLEDTAQ AAGCFLNGRH MGTFGKVGTF
     SFDAVKTLTT GEGGMVITDD ADLWRRASEY HDHGHDHRPV GRGNEGRNFF GFNFRMMELQ
     GAIGLAQLAK MPAMVQTYQK HKNAMLEALG QVPGLSPRRV ADRSGDAATF VSWFLPDAQA
     AARFNKSLAD SGCGAVPWGV NTWHSYPNWE QLHAGATPIA SGWPFKRPGG ADLRFGPADL
     PNTKELLGRC LSWQIMLNWD DAKIEAMRQA VAKAAKEL
//
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