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Database: UniProt
Entry: B3ELM3_CHLPB
LinkDB: B3ELM3_CHLPB
Original site: B3ELM3_CHLPB 
ID   B3ELM3_CHLPB            Unreviewed;       387 AA.
AC   B3ELM3;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ACE03352.1};
DE            EC=2.6.1.50 {ECO:0000313|EMBL:ACE03352.1};
GN   OrderedLocusNames=Cphamn1_0386 {ECO:0000313|EMBL:ACE03352.1};
OS   Chlorobium phaeobacteroides (strain BS1).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE03352.1};
RN   [1] {ECO:0000313|EMBL:ACE03352.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS1 {ECO:0000313|EMBL:ACE03352.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP001101; ACE03352.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3ELM3; -.
DR   STRING; 331678.Cphamn1_0386; -.
DR   KEGG; cpb:Cphamn1_0386; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_7_0_10; -.
DR   OrthoDB; 9810913at2; -.
DR   GO; GO:0047310; F:glutamine-scyllo-inositol transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ACE03352.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:ACE03352.1}.
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         183
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   387 AA;  43088 MW;  EF6A41813E1567DB CRC64;
     MMSFPYWPSY SREEAEVASR VLLSNKVNYW TGNEGRAFEK EFAGYCGCRY AVALCNGTAA
     LELALRALGI GMGDEVIVPC YTFIATASAV VACGAVPVMA DVDRDSLTIT AETVAPRITS
     RTKAVIPVHL MGYPCDMDPI LMLSEKHGLK VVEDCAQAHG ARYKGRSVGT IGDIGAWSFC
     QDKIMTTAGE GGMVTTDNEV YREKMWSYKD HGKSWKAVYG KKHSPGFRWV HESFGTNWRM
     TEIQAAIGRI QLSRMPLWQA QRKRNASILS DGFRSIPGIE VQEQNPDIVH AYYKYATFLE
     TDILRFSGGR EAVMEAVNAS GVPCFSGVCP EIYREKAFEQ ANLVPPERMP AAHEMGKRSL
     VFQVHPALQE QHMYRTVEVV RQVLSQL
//
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