ID A0A0Q7AQ11_9BURK Unreviewed; 495 AA.
AC A0A0Q7AQ11;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=O-acetylserine lyase {ECO:0000313|EMBL:KQW37709.1};
GN ORFNames=ASC76_06290 {ECO:0000313|EMBL:KQW37709.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW37709.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW37709.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW37709.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW37709.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW37709.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|PIRSR:PIRSR605856-50};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004895}.
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:KQW37709.1}.
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DR EMBL; LMDS01000004; KQW37709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7AQ11; -.
DR STRING; 1736528.ASC76_06290; -.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000051611; Unassembled WGS sequence.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR CDD; cd02066; GRX_family; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR005859; CysK.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01139; cysK; 1.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00291; PALP; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KQW37709.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT DOMAIN 7..312
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT DOMAIN 380..447
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT BINDING 73
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 177..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 285
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 43
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 495 AA; 52850 MW; 5CE57F3A566A0168 CRC64;
MSRHDNILQT IGNTPLVRLN KLAPEGVHVH VKLESFNPLG SVKDRMALAV IEDAERRGVL
KPGQTVVEAT SGNTGIGLAM VCAQRGYPLV LTMAESFSLE RRKLLRFLGA RVVLTPAAEK
GTGMLNKAIE LAEAHGWFLC RQFDNQANAD VHTRTTAQEI LADFEGERIH AFVSGFGTGG
TLLGVARGLK AADAGIRVIA AEPDNAPLLG SGIAQQRDGA GRPSASHPMF RPHLMQGWSP
DFISGLVETA VSERLIDEIV PVNGNEALLL ARRLATQEGI FVGTSSGATL AAALEVAKRA
PPGSHIVCML PDTGERYLST PLFDGIGVDM NDEELALSRS TPGYRFDASP GAALAAPAPA
STLDPQAEAL VTQAVQDNAV VMFALEWCEF CWAARKLFAR MGIAFKSVDI DSVTYQQNDM
GAKIRAVLKQ RTGAPTIPQI WIGGVHVGGA MDLFDAARSG RAHQLLARAD VAVESGVPID
PDEFLPKWLH PRKAA
//
