SDHAB_BACSU
ID SDHAB_BACSU Reviewed; 220 AA.
AC O34635;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable L-serine dehydratase, beta chain;
DE Short=SDH;
DE EC=4.3.1.17;
DE AltName: Full=L-serine deaminase;
DE Short=L-SD;
GN Name=sdaAB; Synonyms=yloW; OrderedLocusNames=BSU15850;
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}.
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DR EMBL; Y13937; CAA74258.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13458.1; -; Genomic_DNA.
DR PIR; F69879; F69879.
DR RefSeq; NP_389467.1; NC_000964.3.
DR RefSeq; WP_003232050.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34635; -.
DR SMR; O34635; -.
DR IntAct; O34635; 1.
DR STRING; 224308.BSU15850; -.
DR jPOST; O34635; -.
DR PaxDb; O34635; -.
DR EnsemblBacteria; CAB13458; CAB13458; BSU_15850.
DR GeneID; 935964; -.
DR KEGG; bsu:BSU15850; -.
DR PATRIC; fig|224308.179.peg.1725; -.
DR eggNOG; COG1760; Bacteria.
DR InParanoid; O34635; -.
DR OMA; HTAGACR; -.
DR PhylomeDB; O34635; -.
DR BioCyc; BSUB:BSU15850-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 Gene3D; 3.30.1330.90; -; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR029009; ASB_dom_sf.
DR InterPro; IPR004643; Fe-S_L-Ser_bsu.
DR InterPro; IPR005131; Ser_deHydtase_bsu.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF03315; SDH_beta; 1.
DR PIRSF; PIRSF036692; SDH_B; 1.
DR SUPFAM; SSF143548; SSF143548; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR00719; sda_beta; 1.
DR PROSITE; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Gluconeogenesis; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..220
FT /note="Probable L-serine dehydratase, beta chain"
FT /id="PRO_0000171916"
FT DOMAIN 148..220
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 220 AA; 23819 MW; 2BDEB5CF70C2D1CD CRC64;
MKYRSVFDII GPVMIGPSSS HTAGAARIGR VARSLFGREP ERIIVSFYGS FAETYKGHGT
DVAIIGGLLD FDTFDERIKT AIQIAEAKGI DIEFRVEDAV PVHPNTAKIT ISDEKGELEL
TGISIGGGKI EITELNGFEL RLSGNHPAIL VVHNDKFGTI AGVANVLAKF SINVGHMEVA
RKDIGQLALM TIEVDQNIDD HILDELSKLP NIIQVTKIAD
