ID A0A1B9EYR6_9ACTN Unreviewed; 404 AA.
AC A0A1B9EYR6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:OCC12641.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:OCC12641.1};
GN Name=mccB {ECO:0000313|EMBL:OCC12641.1};
GN ORFNames=A3Q37_01304 {ECO:0000313|EMBL:OCC12641.1};
OS Streptomyces sp. PTY087I2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1819298 {ECO:0000313|EMBL:OCC12641.1, ECO:0000313|Proteomes:UP000093256};
RN [1] {ECO:0000313|EMBL:OCC12641.1, ECO:0000313|Proteomes:UP000093256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTY087I2 {ECO:0000313|EMBL:OCC12641.1,
RC ECO:0000313|Proteomes:UP000093256};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|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:OCC12641.1}.
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DR EMBL; LZRD01000005; OCC12641.1; -; Genomic_DNA.
DR RefSeq; WP_065478833.1; NZ_LZRD01000005.1.
DR AlphaFoldDB; A0A1B9EYR6; -.
DR Proteomes; UP000093256; 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:0009058; P:biosynthetic process; IEA:UniProt.
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:SF85; 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 Lyase {ECO:0000313|EMBL:OCC12641.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000093256}.
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 404 AA; 42484 MW; F049E368C4B5C28C CRC64;
MDNEVSMTPL APTPSRALAT EAVHAGRDDL ASLGVHAPPI DLSTTYPSYD SRDEAMRIDA
FATTGSLPDG PPVYARLDNP TTGRFETALA RLEGTDSAVA FASGMAALTA VLLARASQGL
RHVVAVRPLY GCSDHLLGAG LLGTEVTWTD PAGIADAIRP DTGLVMVETP ANPTLAEVDI
RAVAHACGTV PLLVDNTFAT PVLQRPVEHG ARIVLHSATK YLGGHGDVMG GVVACDEEFA
ATLRQVRFAT GGVLHPLAGY LLLRGLSTLP VRVRAASTSA AELVRRLTAD PRIARVHYPR
IGGAMISFEV YGDPHRVISG VRLITPAVSL GSVDSLIQHP ASISHRIVEE GDRRAAGVGD
RLLRMSVGLE DVEDLWADLC QALSDGPVPS ARTAERPLHS SAGR
//