ID A0A0J6NK12_9NEIS Unreviewed; 381 AA.
AC A0A0J6NK12;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Putative 8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00021531};
GN ORFNames=VK98_11435 {ECO:0000313|EMBL:KMN81728.1};
OS Chromobacterium sp. LK11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN81728.1, ECO:0000313|Proteomes:UP000036114};
RN [1] {ECO:0000313|EMBL:KMN81728.1, ECO:0000313|Proteomes:UP000036114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LK11 {ECO:0000313|EMBL:KMN81728.1,
RC ECO:0000313|Proteomes:UP000036114};
RA Chan X.Y.;
RT "Draft genome of Chromobacterium aquaticum LK11.";
RL Submitted (MAY-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:KMN81728.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDUR01000016; KMN81728.1; -; Genomic_DNA.
DR RefSeq; WP_048414147.1; NZ_LDUR01000016.1.
DR AlphaFoldDB; A0A0J6NK12; -.
DR STRING; 1628212.VK98_11435; -.
DR PATRIC; fig|1628212.3.peg.1240; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000036114; 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:UP000036114}.
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 381 AA; 41257 MW; F6BC3D866A9DB21E CRC64;
MKFATRSIHV GYDNADHGKA VMPPVYQTSV FEYGHVGESM PFVYARTGNP TRAALEACLA
SLENARHGLA FASGMAAIDA VLRACLKPGD EVIAVADLYG GAYRLLTKVM EPAGVKVVFA
DLSDSRKLET LISARTKLLW LESPTNPLLG MVDIAELAKT AHAHGVRVAV DSTFATPYLQ
NPLDLGADIV VHSATKYLAG HSDVLLGLVA VSDDALHREI KFIQNAAGAV PGPQDCFLTL
RGIKTLHLRM DRHCDNAERV ADYLQSHPKV ERVFFPGLPE HPGHDLAGRQ MRRFGGIVSI
WLKDDSREAA SRLAERLRLF ALAESLGGVE SLINHSYTMS HGGMPPEQKA QLGIREGGVR
LSIGIEDIDD ILADLEQALA D
//
