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Database: UniProt
Entry: Q89LU8_BRADU
LinkDB: Q89LU8_BRADU
Original site: Q89LU8_BRADU 
ID   Q89LU8_BRADU            Unreviewed;       394 AA.
AC   Q89LU8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Cystathionine beta lyase {ECO:0000313|EMBL:BAC49710.1};
GN   Name=metC {ECO:0000313|EMBL:BAC49710.1};
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC49710.1, ECO:0000313|Proteomes:UP000002526};
RN   [1] {ECO:0000313|Proteomes:UP000002526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC   {ECO:0000313|Proteomes:UP000002526};
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000256|ARBA:ARBA00001535};
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; BA000040; BAC49710.1; -; Genomic_DNA.
DR   RefSeq; NP_771085.1; NC_004463.1.
DR   RefSeq; WP_011087217.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89LU8; -.
DR   STRING; 224911.AAV28_19385; -.
DR   EnsemblBacteria; BAC49710; BAC49710; BAC49710.
DR   GeneID; 64024190; -.
DR   KEGG; bja:bll4445; -.
DR   PATRIC; fig|224911.44.peg.4214; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_5_1_5; -.
DR   InParanoid; Q89LU8; -.
DR   OrthoDB; 9790858at2; -.
DR   PhylomeDB; Q89LU8; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IBA:GO_Central.
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; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
DR   PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR   PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 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:BAC49710.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   394 AA;  42667 MW;  FC9EFE8C5FA5986E CRC64;
     MDSSHPSQQQ AETRLVTSGR DTKAQKGFVN PPVFHGSTVL YPTAEDLHAH RGEFTYGRHG
     TPTTRAFQDT LMALEGPQCA GVGIVPSGLS AISTTLLSVL KTGDHILVCD NVYRPSRNFC
     NGMLARYGVE TTYFDPLIGA GIDKLFKPNT RAVLVEAPGS QSFEMPDIRA IAEVAHARDA
     LVIDDNTWAT PLYHRSLEQG VDISMQAATK YIGGHSDIMF GTISANAKAW PQIAEGIRLL
     GVCAGPDDVF LALRGLRTLS VRLAQHHRSG LDMARWLASR PEVARVLHPG LETDPGHAIW
     KRDFTGASGL FSIVLKPAPQ KAVDTMLNTL KLFGMGFSWG GFESLAIPFD CDGYRTATKW
     APGGPTLRLH IGLESTDDLK ADLDRGFAAL KTAM
//
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