ID A0A0Q7DC48_9CAUL Unreviewed; 391 AA.
AC A0A0Q7DC48;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KQW71088.1};
GN ORFNames=ASC73_13720 {ECO:0000313|EMBL:KQW71088.1};
OS Phenylobacterium sp. Root1277.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW71088.1, ECO:0000313|Proteomes:UP000051150};
RN [1] {ECO:0000313|EMBL:KQW71088.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71088.1,
RC ECO:0000313|Proteomes:UP000051150};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW71088.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71088.1,
RC ECO:0000313|Proteomes:UP000051150};
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|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:KQW71088.1}.
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DR EMBL; LMDZ01000005; KQW71088.1; -; Genomic_DNA.
DR RefSeq; WP_056023493.1; NZ_LMDZ01000005.1.
DR AlphaFoldDB; A0A0Q7DC48; -.
DR Proteomes; UP000051150; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KQW71088.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051150}.
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 391 AA; 42190 MW; 70203814282CF959 CRC64;
MTQDTTGKNR LEFSTRVIHG GQSVDPTTGA VMPPIYATST YAQASPGEHK GFEYSRSQNP
TRFAFERAIA DLESGTRGYA FASGLAAIST FLEVLDAGDH VIASEDLYGG SFRLFDKVRK
RTAALEFSFV DMSDVAAIEA AIRPNTKLIW VETPTNPLLR LADLEAIAQL GKRRGLLTAA
DNTFASPYVQ RPLEFGFDAV MHSTTKYVSG HSDIVGGALV VGRNKDLADQ VGFLQNAVGA
VSSPFDSFLA LRGVKTLALR MQRHCENGMA IARWLEARPD VAKVIYPGLE SHPQHELAKR
QMSGGFGGMI SAVLDRDLAG TVRMLERTRL FTLAESLGGV ESLIEHPAIM THASIPAETR
ARIGIADGLI RLSVGIEDVG DLIADLEQAL A
//
