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Database: UniProt
Entry: C6HWB2_9BACT
LinkDB: C6HWB2_9BACT
Original site: C6HWB2_9BACT 
ID   C6HWB2_9BACT            Unreviewed;       376 AA.
AC   C6HWB2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:EES53090.1};
GN   ORFNames=UBAL3_80420040 {ECO:0000313|EMBL:EES53090.1};
OS   Leptospirillum ferrodiazotrophum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=412449 {ECO:0000313|EMBL:EES53090.1, ECO:0000313|Proteomes:UP000009374};
RN   [1] {ECO:0000313|EMBL:EES53090.1, ECO:0000313|Proteomes:UP000009374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19429552; DOI=10.1128/AEM.02943-08;
RA   Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M.,
RA   Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J.,
RA   Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., Banfield J.F.;
RT   "Community genomic and proteomic analyses of chemoautotrophic iron-
RT   oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum
RT   ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.";
RL   Appl. Environ. Microbiol. 75:4599-4615(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR   EMBL; GG693869; EES53090.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HWB2; -.
DR   Proteomes; UP000009374; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009374}.
FT   DOMAIN          30..362
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   376 AA;  40868 MW;  50B4E86374DF6479 CRC64;
     MEEPIASLIE IGYSALEISG RFKTMPPPGL VSLSSNDYLG LSRNPLVIDA SLRATRNFGT
     GATGSRYLSG NHPLNRELSD ATSQFKTGGK GAALVFTSGY HANLATVSLI SELSPLIFSD
     SENHASLIDG MRNAKGRKVV YPHNESEFIR EYLKKNPQQK PVIVTESLFS MKGDLAPLSA
     LFEIVEEYDG MLVIDEAHAT GTTGISGRGA LEALGLPYVP ERMILTGTYS KALGSLGGFV
     ILHEKAAKIL ESTARTLIYT TALPPGVLAA SLEAIHVLAE NTEIVRSLQR ESRIWNAYIQ
     DDTESSSPII PVMGDAPTLQ SVSDNFRTQG YYLPVITYPT VPRGEDLLRL SVNIGWDKNV
     RKTLETFLPP RKGVQK
//
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