ID G6AXM9_9BACT Unreviewed; 390 AA.
AC G6AXM9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Cys/Met metabolism PLP-dependent enzyme {ECO:0000313|EMBL:EHJ40255.1};
GN ORFNames=HMPREF0673_01385 {ECO:0000313|EMBL:EHJ40255.1};
OS Leyella stercorea DSM 18206.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Leyella.
OX NCBI_TaxID=1002367 {ECO:0000313|EMBL:EHJ40255.1, ECO:0000313|Proteomes:UP000004407};
RN [1] {ECO:0000313|EMBL:EHJ40255.1, ECO:0000313|Proteomes:UP000004407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18206 {ECO:0000313|EMBL:EHJ40255.1,
RC ECO:0000313|Proteomes:UP000004407};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHJ40255.1}.
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DR EMBL; AFZZ01000122; EHJ40255.1; -; Genomic_DNA.
DR RefSeq; WP_007899458.1; NZ_JH379419.1.
DR AlphaFoldDB; G6AXM9; -.
DR GeneID; 78337065; -.
DR PATRIC; fig|1002367.3.peg.1108; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_10; -.
DR Proteomes; UP000004407; 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 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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 390 AA; 43262 MW; E2B6B38514144C34 CRC64;
MKKQTIAIDT PFQKSDAYGA LSMPVYHTLA YEFADADVMS DAFCGRIEEP DYSRVMNPTV
NYLELKIKAL TGADRVTAMS SGMAAISGTL ISLAEQGKNV VASRHMFGNT YSLLTKTLPR
FGVTTHLCDL TNLDEVRRAV DADTCCIFLE IITNPQLEVA DLTALAEIAH AHNIPLVADT
TAIPFTEFCA HELGVDIEVV STTKYLSGGA TSLGGMVIDY GGFPEFARRL HDEMLFNLGA
YMTPHVAYMQ NLGLENLRAR YDLQVRNTVY LVNALRQMEG IKSVNYVGLP DNPYYELAQR
QFGKTAGCMF TIDLESKEAC FRFINNLKLV HRATNLFDNR TLAIHPASTI FGPFSDEQRA
AMDVLDTTIR ISVGLEDMDD IIEDFRQALL
//
