SDHAA_BACSU
ID SDHAA_BACSU Reviewed; 300 AA.
AC O34607;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable L-serine dehydratase, alpha chain;
DE Short=SDH;
DE EC=4.3.1.17;
DE AltName: Full=L-serine deaminase;
DE Short=L-SD;
GN Name=sdaAA; Synonyms=ylpA; OrderedLocusNames=BSU15860;
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=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC family. {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; Y13937; CAA74259.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13459.1; -; Genomic_DNA.
DR PIR; G69879; G69879.
DR RefSeq; NP_389468.1; NC_000964.3.
DR RefSeq; WP_003232049.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34607; -.
DR SMR; O34607; -.
DR STRING; 224308.BSU15860; -.
DR PaxDb; O34607; -.
DR PRIDE; O34607; -.
DR EnsemblBacteria; CAB13459; CAB13459; BSU_15860.
DR GeneID; 937109; -.
DR KEGG; bsu:BSU15860; -.
DR PATRIC; fig|224308.179.peg.1726; -.
DR eggNOG; COG1760; Bacteria.
DR InParanoid; O34607; -.
DR OMA; FVEVPCV; -.
DR PhylomeDB; O34607; -.
DR BioCyc; BSUB:BSU15860-MON; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005130; Ser_deHydtase-like_asu.
DR InterPro; IPR004642; Ser_deHydtase_asu.
DR Pfam; PF03313; SDH_alpha; 1.
DR TIGRFAMs; TIGR00718; sda_alpha; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Gluconeogenesis; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..300
FT /note="Probable L-serine dehydratase, alpha chain"
FT /id="PRO_0000171912"
SQ SEQUENCE 300 AA; 30936 MW; 244239DA147CB014 CRC64;
MFRNVKELIE ITKEKQILIS DVMIAQEMEV TEKTKEDIFQ QMDHNLSVME AAVQKGLEGV
TSQTGLTGGD AVKLQAYIRS GKSLSGPLIL DAVSKAVATN EVNAAMGTIC ATPTAGSAGV
VPGTLFAVKE KLNPTREQMI RFLFTAGAFG FVVANNASIS GAAGGCQAEV GSASGMAAAA
IVEMAGGTPE QSAEAMAITL KNMLGLVCDP VAGLVEVPCV KRNAMGASNA MIAADMALAG
ITSRIPCDEV IDAMYKIGQT MPTALRETGQ GGLAATPTGR ELEKKIFGGA LGSRETTSAN