ID F9DT80_9BACL Unreviewed; 397 AA.
AC F9DT80;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EGQ25996.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:EGQ25996.1};
GN Name=metC2 {ECO:0000313|EMBL:EGQ25996.1};
GN ORFNames=HMPREF9372_2011 {ECO:0000313|EMBL:EGQ25996.1};
OS Sporosarcina newyorkensis 2681.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1027292 {ECO:0000313|EMBL:EGQ25996.1, ECO:0000313|Proteomes:UP000005316};
RN [1] {ECO:0000313|EMBL:EGQ25996.1, ECO:0000313|Proteomes:UP000005316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2681 {ECO:0000313|EMBL:EGQ25996.1,
RC ECO:0000313|Proteomes:UP000005316};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (APR-2011) 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:EGQ25996.1}.
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DR EMBL; AFPZ01000064; EGQ25996.1; -; Genomic_DNA.
DR AlphaFoldDB; F9DT80; -.
DR STRING; 759851.SAMN04244570_3534; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_9; -.
DR Proteomes; UP000005316; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
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:SF91; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EGQ25996.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 397 AA; 44346 MW; 75B875090D0000AF CRC64;
MFEGLFEMKR LFFIFLKGMD TMTNNELETR LVQLGNNSDK KTGAVNTPIY LSTAYHHEGL
GQSTGYDYTR TKNPTRSILE DGIADLESGD QGYACSSGMA AIQLILSLFK TGDEILAPED
LYGGTYRLFQ QYEKTYQIST HYLTFEDVSE VEQAITDRTK AIFLETPTNP LMLQINVATY
AELAKKHGLL LIVDNTFLTP YFQRPIEEGA DIVIHSATKY IGGHNDVLAG LVVAKGEELC
DRLFTNHNAS GATLSPFDSW LVVRGLKTLH LRMKQHDANA KEMVAYLKQE PLIADVLYAG
IGGMLSFRVQ NSEWVGPFLE NMKLISFAES LGGVESFITY PTTQTHMDIP IEERNRRGVD
DRLLRFSVGV EDADDLIADV KQALYAAKEA VEAVNIH
//
