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Database: UniProt
Entry: A0A402AUG5_9CHLR
LinkDB: A0A402AUG5_9CHLR
Original site: A0A402AUG5_9CHLR 
ID   A0A402AUG5_9CHLR        Unreviewed;       445 AA.
AC   A0A402AUG5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:GCE22689.1};
GN   ORFNames=KDK_64890 {ECO:0000313|EMBL:GCE22689.1};
OS   Dictyobacter kobayashii.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Dictyobacter.
OX   NCBI_TaxID=2014872 {ECO:0000313|EMBL:GCE22689.1, ECO:0000313|Proteomes:UP000287188};
RN   [1] {ECO:0000313|Proteomes:UP000287188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno11 {ECO:0000313|Proteomes:UP000287188};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) 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:GCE22689.1}.
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DR   EMBL; BIFS01000002; GCE22689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402AUG5; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000287188; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 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:UP000287188};
KW   Transferase {ECO:0000313|EMBL:GCE22689.1}.
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   445 AA;  48434 MW;  86793E432077E056 CRC64;
     MPEIDGDHVF GFDTLALHAG QRPDPTTGAQ AVPIYQTTSY IFDDTDHAAH LFALQRFGNI
     YTRIMNPTTA AFEERIAALE GGTGAVATAS GMAAQMAVMM TLLRPGDELV AASNLYGGTH
     TQFDLTLRTW GINTIFVDST DPENFRRALT PKTRAFYGET IGNPGGDVLD IRTIADIAHE
     AGVPLIIDNT FATPYLCRPF EHGADIVVHS ATKFIGGHGT SIGGVLIENG KFPWDNGKFA
     HIVDPSPGYH GVRFYETFGD FCFVMKARVE TVRDTGPSLS PFNSFLLLQG LETLSLRMDR
     HCQNALQVAR FLQEHPAVSW VRYSGLPEDR SHELAKHYLP RGGGAIFTFG VKGGYEAGKA
     VINNVRLFAH LANVGDARSL IIHPASTTHQ QLSEEDLLAG GVTPDLIRLS IGLENIEDIL
     WDLDQALGKA TANVQKNRDT EKGAE
//
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