MCCA_BACSU
ID MCCA_BACSU Reviewed; 307 AA.
AC O05393; Q795Y2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=O-acetylserine dependent cystathionine beta-synthase;
DE EC=2.5.1.134 {ECO:0000269|PubMed:17056751};
GN Name=mccA; Synonyms=yrhA; OrderedLocusNames=BSU27260;
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, INDUCTION, AND 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 O-acetylserine and homocysteine
CC to cystathionine. {ECO:0000269|PubMed:17056751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + O-acetyl-L-serine = acetate + H(+) + L,L-
CC cystathionine; Xref=Rhea:RHEA:32743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58340; EC=2.5.1.134;
CC Evidence={ECO:0000269|PubMed:17056751};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- INDUCTION: By methionine. Repressed by sulfate and cysteine.
CC {ECO:0000269|PubMed:17056751}.
CC -!- DISRUPTION PHENOTYPE: Grows very slowly with methionine as sole sulfur
CC source. {ECO:0000269|PubMed:17056751}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; U93874; AAB80858.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14668.1; -; Genomic_DNA.
DR PIR; H69973; H69973.
DR RefSeq; NP_390604.1; NC_000964.3.
DR RefSeq; WP_003229809.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O05393; -.
DR SMR; O05393; -.
DR STRING; 224308.BSU27260; -.
DR PaxDb; O05393; -.
DR PRIDE; O05393; -.
DR EnsemblBacteria; CAB14668; CAB14668; BSU_27260.
DR GeneID; 937576; -.
DR KEGG; bsu:BSU27260; -.
DR PATRIC; fig|224308.179.peg.2962; -.
DR eggNOG; COG0031; Bacteria.
DR InParanoid; O05393; -.
DR OMA; WMADYGF; -.
DR PhylomeDB; O05393; -.
DR BioCyc; BSUB:BSU27260-MON; -.
DR SABIO-RK; O05393; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IDA:CAFA.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:CAFA.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:CAFA.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:CAFA.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="O-acetylserine dependent cystathionine beta-
FT synthase"
FT /id="PRO_0000360653"
FT BINDING 74
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 178..182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 307 AA; 33019 MW; 3F38C347F4EB1461 CRC64;
MTVITDITEL IGNTPLLRLK NFDVPEGVAV YAKLEMMNPG GSIKDRLGDM LIRDALDSGK
VKPGGVIIEA TAGNTGIGLA LSARKYGLKA IFCVPEHFSR EKQQIMQALG ASIIHTPRQD
GMQGAIQKAI QLETEIENSY CVLQFKNRVN PSTYYKTLGP EMWEALDGNI HTFVAGAGSG
GTFAGTASFL KEKNPAVKTV IVEPVGSILN GGEPHAHKTE GIGMEFIPDY MDKSHFDEIY
TVTDENAFRL VKEAAEKEGL LIGSSSGAAL YAALEEAKKA SAGTNIVTVF PDSSDRYISK
QIYEGGI
