ID A0A0M2K608_9MYCO Unreviewed; 373 AA.
AC A0A0M2K608;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:KKF02621.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:KKF02621.1};
GN ORFNames=WN67_07275 {ECO:0000313|EMBL:KKF02621.1};
OS Mycolicibacterium obuense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF02621.1, ECO:0000313|Proteomes:UP000034150};
RN [1] {ECO:0000313|EMBL:KKF02621.1, ECO:0000313|Proteomes:UP000034150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|EMBL:KKF02621.1,
RC ECO:0000313|Proteomes:UP000034150};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium obuense UC1.";
RL Submitted (APR-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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {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:KKF02621.1}.
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; LAUZ02000008; KKF02621.1; -; Genomic_DNA.
DR RefSeq; WP_046362345.1; NZ_LAUZ02000008.1.
DR AlphaFoldDB; A0A0M2K608; -.
DR STRING; 1807.MOBUDSM44075_05352; -.
DR PATRIC; fig|1807.13.peg.1091; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000034150; Unassembled WGS sequence.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Lyase {ECO:0000313|EMBL:KKF02621.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 373 AA; 39142 MW; D66329F403BFFD38 CRC64;
MTYGETYGDS TRSLKAIAAE HVPGDPVGPV PVPAAAYHLG ADEDDALDSY GRRHNPTWRQ
LESALATLEG AAAAVAFGSG MAAITSVLRA VTEPGSTLVV PADGYYQVRA YATEYLAPRG
VTVVQATCAQ MCEAARDADV VLAETPSNPG LDVVDLHRLA MQCRPRGALL LVDNTTATPL
GQQPLALGAD LVVASATKAL SGHHDLLAGY VAGNRADVIE RLQRERLLAG PILGAFEAWL
VLRGLGTLGL RFERQCQNAA AVAMMLRSHP AVTAVRYPGL PDDPSHAIAT RQMRRFGGIV
SVELADADAV HDLVRRSALL VGATSFGGVH TSVDRRARWG DPVSPGFARI SCGIEDTDDL
LADIDSALAG AGR
//
