MCCB_BACSU
ID MCCB_BACSU Reviewed; 379 AA.
AC O05394; Q795Y3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cystathionine gamma-lyase;
DE EC=4.4.1.1;
DE AltName: Full=Gamma-cystathionase;
DE AltName: Full=Homocysteine gamma-lyase;
DE EC=4.4.1.2;
GN Name=mccB; Synonyms=yrhB; OrderedLocusNames=BSU27250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
RA Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
RA Duesterhoeft A., Ehrlich S.D.;
RT "Sequence of the Bacillus subtilis genome region in the vicinity of the lev
RT operon reveals two new extracytoplasmic function RNA polymerase sigma
RT factors SigV and SigZ.";
RL Microbiology 143:2939-2943(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=17056751; DOI=10.1128/jb.01273-06;
RA Hullo M.-F., Auger S., Soutourina O., Barzu O., Yvon M., Danchin A.,
RA Martin-Verstraete I.;
RT "Conversion of methionine to cysteine in Bacillus subtilis and its
RT regulation.";
RL J. Bacteriol. 189:187-197(2007).
CC -!- FUNCTION: Catalyzes the conversion of cystathionine to cysteine, and
CC homocysteine to sulfide. {ECO:0000269|PubMed:17056751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine +
CC NH4(+); Xref=Rhea:RHEA:14005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:35235, ChEBI:CHEBI:58161; EC=4.4.1.1;
CC Evidence={ECO:0000269|PubMed:17056751};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-homocysteine = 2-oxobutanoate + H(+) + hydrogen
CC sulfide + NH4(+); Xref=Rhea:RHEA:14501, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:58199; EC=4.4.1.2;
CC Evidence={ECO:0000269|PubMed:17056751};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 mM for cystathionine {ECO:0000269|PubMed:17056751};
CC Vmax=2 umol/min/mg enzyme for cystathionine gamma-lyase reaction
CC {ECO:0000269|PubMed:17056751};
CC -!- INDUCTION: By methionine. Repressed by sulfate and cysteine.
CC {ECO:0000269|PubMed:17056751}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17056751}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U93874; AAB80859.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14667.1; -; Genomic_DNA.
DR PIR; A69974; A69974.
DR RefSeq; NP_390603.1; NC_000964.3.
DR RefSeq; WP_003229810.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O05394; -.
DR SMR; O05394; -.
DR STRING; 224308.BSU27250; -.
DR PaxDb; O05394; -.
DR PRIDE; O05394; -.
DR EnsemblBacteria; CAB14667; CAB14667; BSU_27250.
DR GeneID; 936947; -.
DR KEGG; bsu:BSU27250; -.
DR PATRIC; fig|224308.179.peg.2961; -.
DR eggNOG; COG0626; Bacteria.
DR InParanoid; O05394; -.
DR OMA; MQTKLIH; -.
DR PhylomeDB; O05394; -.
DR BioCyc; BSUB:BSU27250-MON; -.
DR BRENDA; 2.5.1.134; 658.
DR SABIO-RK; O05394; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IDA:CAFA.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central.
DR GO; GO:0047982; F:homocysteine desulfhydrase 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; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0043418; P:homocysteine catabolic process; IDA:CAFA.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:CAFA.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..379
FT /note="Cystathionine gamma-lyase"
FT /id="PRO_0000360652"
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 40886 MW; 44DD71446F6E15B4 CRC64;
MKKKTLMIHG GITGDEKTGA VSVPIYQVST YKQPKAGQHT GYEYSRTANP TRTALEALVT
ELESGEAGYA FSSGMAAITA VMMLFNSGDH VVLTDDVYGG TYRVMTKVLN RLGIESTFVD
TSSREEVEKA IRPNTKAIYI ETPTNPLLKI TDLTLMADIA KKAGVLLIVD NTFNTPYFQQ
PLTLGADIVL HSATKYLGGH SDVVGGLVVT ASKELGEELH FVQNSTGGVL GPQDSWLLMR
GIKTLGLRME AIDQNARKIA SFLENHPAVQ TLYYPGSSNH PGHELAKTQG AGFGGMISFD
IGSEERVDAF LGNLKLFTIA ESLGAVESLI SVPARMTHAS IPRERRLELG ITDGLIRISV
GIEDAEDLLE DIGQALENI
