ID A9WBP2_CHLAA Unreviewed; 371 AA.
AC A9WBP2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ABY34849.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:ABY34849.1};
GN OrderedLocusNames=Caur_1631 {ECO:0000313|EMBL:ABY34849.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY34849.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP000909; ABY34849.1; -; Genomic_DNA.
DR RefSeq; WP_012257503.1; NC_010175.1.
DR RefSeq; YP_001635238.1; NC_010175.1.
DR AlphaFoldDB; A9WBP2; -.
DR STRING; 324602.Caur_1631; -.
DR EnsemblBacteria; ABY34849; ABY34849; Caur_1631.
DR KEGG; cau:Caur_1631; -.
DR PATRIC; fig|324602.8.peg.1867; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_0; -.
DR InParanoid; A9WBP2; -.
DR Proteomes; UP000002008; Chromosome.
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 GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IBA:GO_Central.
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:ABY34849.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW Transferase {ECO:0000313|EMBL:ABY34849.1}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 371 AA; 40696 MW; 4AAD1DE8934AD10A CRC64;
MIPFVDLKAQ YLSIKEEIDR AVLDTLASTQ FVLGKEVVAF EELFAAYTQS QYALGVNSGT
SALHLALLAC GVGPGDEVIT TPHTFIATVS AIDYTGARPV FVDIDPVTFT VNPALIEAAI
TPRTKAIIPV HLYGQPADMD PIMAIARKHN LVVIEDAAQA HGAEYKGRRV GSIGDAGCFS
FYPGKNLGAY GEGGAVTTNN PEIARTVRML RDWGAERRYH HDLKGFNYRM EGVQGAILRV
KMAYIEHWTE LRRAAAARYD AMLAPLGIQT PVALPDRRHV YHIYAIRDRQ RDALQTYLHD
HGVSTGIHYP IPVHLQKAFA DLGYRVGDFP QAELAAAEVL SLPMFPELTV DQQQVVAEAL
QGWMQQVAAG C
//
