ID   A0A0J5GD40_9NEIS        Unreviewed;       381 AA.
AC   A0A0J5GD40;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Putative 8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00021531};
GN   ORFNames=ACG97_13870 {ECO:0000313|EMBL:KMJ52394.1};
OS   Vogesella sp. EB.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ52394.1, ECO:0000313|Proteomes:UP000054352};
RN   [1] {ECO:0000313|EMBL:KMJ52394.1, ECO:0000313|Proteomes:UP000054352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB {ECO:0000313|EMBL:KMJ52394.1,
RC   ECO:0000313|Proteomes:UP000054352};
RA   Arrua Day P., Revale S., Alvarez H.M.;
RT   "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT   Vogesella sp. strain EB.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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:KMJ52394.1}.
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DR   EMBL; LFDT01000028; KMJ52394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J5GD40; -.
DR   STRING; 1526735.ACG97_13870; -.
DR   PATRIC; fig|1526735.3.peg.2954; -.
DR   Proteomes; UP000054352; Unassembled WGS sequence.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054352}.
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   381 AA;  40543 MW;  B105764DF4D27EEB CRC64;
     MKFATKAIHA GFDYHQHNRA VMPPIYQTSA FAHDAVGESL EFAYARTGTP TRAALEANFA
     ALEDAAHGLA FASGMAAIDA VLRATLKPGD EVIAVADLYG GAYRILDKVL AAQGIKVTFA
     DLSDAANLEA VISSNTRLLW LETPTNPLLG MVDIAALAAI AHSHGAVVAV DNTFATPYLQ
     NPLNQGADIV VHSATKYLGG HSDVLLGLVA VNDAALFKAI KFIQNAAGAV PGPQDCFLTL
     RGIKTLALRM ERHCDNAEKV AAFLQNHPAI DKVFFPGLPE HPGHELAKRQ MRRFGGIVTV
     YLKEDSRAAA SRVASRLQLF LLAESLGGVE SLVNHSYTMS HGGMPPEQKA ALGIREGQLR
     LSIGIEDIDD ILADLAQALA E
//