ID A0A0S2HZ02_9BACT Unreviewed; 425 AA.
AC A0A0S2HZ02;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:ALO15202.1};
DE EC=4.4.1.11 {ECO:0000313|EMBL:ALO15202.1};
GN Name=mdeA {ECO:0000313|EMBL:ALO15202.1};
GN ORFNames=L21SP5_01556 {ECO:0000313|EMBL:ALO15202.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO15202.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO15202.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO15202.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
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}.
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DR EMBL; CP013118; ALO15202.1; -; Genomic_DNA.
DR RefSeq; WP_057952681.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2HZ02; -.
DR STRING; 1307839.L21SP5_01556; -.
DR KEGG; blq:L21SP5_01556; -.
DR PATRIC; fig|1307839.3.peg.1654; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000064893; Chromosome.
DR GO; GO:0018826; F:methionine gamma-lyase activity; IEA:UniProtKB-EC.
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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ALO15202.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 425 AA; 46587 MW; E8008C0617EF26BB CRC64;
MHFQTKQIHS GYKKDDSTGA RVTPIYQSNA FYFNDSEHAK RLFSLEESGN IYSRLGNPTN
AILESRIADM ENGAAALAVA SGHAAQLITV TTLAKQGDNI VTAPFLYGGT HNQFNVTFRN
FGIDVRFTKD LGAKSFESLI DANTKAIYLE TIGNPSFRIP DFEKLVEVAN KYEIPVVVDN
TFGAGGHFCR PIDYGVHIVL HSATKWIGGH GTSMGGIIID GGQFDWSNER FPLLNQPSPG
YHGINFSETF GELAFIARAR AELLRDLGPV QSSFNSFLLL QGLETLSLRA QKQAENAKEL
AQYLNKHEQV KDVCYPGLEN HPSHKEAQKY LDNGYGAVLS FTVNGGAKSA SFIIDHLELA
GHMANVGDNR TLVIQPAITT HQQLTPEQQK AAGVEAAQIR VSCGIEHSGD IINDFKNALF
KLQSK
//
