ID G9A5M2_RHIFH Unreviewed; 408 AA.
AC G9A5M2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:CCE95700.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:CCE95700.1};
GN Name=metC {ECO:0000313|EMBL:CCE95700.1};
GN OrderedLocusNames=SFHH103_01202 {ECO:0000313|EMBL:CCE95700.1};
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE95700.1, ECO:0000313|Proteomes:UP000007735};
RN [1] {ECO:0000313|EMBL:CCE95700.1, ECO:0000313|Proteomes:UP000007735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103 {ECO:0000313|EMBL:CCE95700.1,
RC ECO:0000313|Proteomes:UP000007735};
RX PubMed=22374952; DOI=10.1128/JB.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(2012).
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; HE616890; CCE95700.1; -; Genomic_DNA.
DR AlphaFoldDB; G9A5M2; -.
DR STRING; 1117943.SFHH103_01202; -.
DR KEGG; sfh:SFHH103_01202; -.
DR PATRIC; fig|380.5.peg.1279; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_5_1_5; -.
DR Proteomes; UP000007735; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:CCE95700.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 408 AA; 44104 MW; 42421E17BF58F5C8 CRC64;
MSFHRVFNGG FVKMADKMSA RGEIGINTRL AHTGNNPSDF HGFVNPPVVH ASTVLFPNAK
AMETRAQKYT YGTRGTPTTD ALCDAINELE GAAGTILVPS GLAAVTVPFL TYLSSGDHAL
IVDSVYFPTR HFCDTMLTRL GVTVEYYDPM IGAAIESLIR PNTRLVHTEA PGSNTFEMQD
IRAIADAGHR HGCVVTMDNT WATPLYFRPL DHGVDVSIHA ATKYPSGHSD VLLGTVSANA
AHWPALTEAM VTLGVCVSPD DSYQILRGLR TMGIRLERHQ ESALALARWL ESREEVARVL
HPALPSFPGH ELWKRDFGGA SGIFSFVLKA EPETSKAKAH AFLDALSFFG LGYSWGGFES
LALHVNLSDR KVAKAPSGGP VIRLQIGLED VADLRRDIEA GLAAANAV
//
