ID   SDHL_STRCO              Reviewed;         455 AA.
AC   O86564;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=L-serine dehydratase;
DE            Short=SDH;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
DE            Short=L-SD;
GN   Name=sdaA; OrderedLocusNames=SCO5469; ORFNames=SC2A11.03c;
OS   Streptomyces coelicolor.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   MEDLINE=21996410; PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- CATALYTIC ACTIVITY: L-serine = pyruvate + NH(3).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (Probable).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine
CC       dehydratase family.
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DR   EMBL; AL939123; CAA20172.1; -; Genomic_DNA.
DR   PIR; T34749; T34749.
DR   RefSeq; NP_629605.1; -.
DR   GeneID; 1100909; -.
DR   GenomeReviews; AL645882_GR; SCO5469.
DR   KEGG; sco:SCO5469; -.
DR   NMPDR; fig|100226.1.peg.5421; -.
DR   HOGENOM; O86564; -.
DR   OMA; O86564; PFVEKEH.
DR   BioCyc; SCOE100226:SCO5469-MON; -.
DR   BRENDA; 4.3.1.17; 1084.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR004644; Fe-S_L-Ser_mono.
DR   InterPro; IPR005130; Ser_deHydtase_asu.
DR   InterPro; IPR005131; Ser_deHydtase_bsu.
DR   Pfam; PF03313; SDH_alpha; 1.
DR   Pfam; PF03315; SDH_beta; 1.
DR   TIGRFAMs; TIGR00720; sda_mono; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Gluconeogenesis; Iron; Iron-sulfur; Lyase;
KW   Metal-binding.
FT   CHAIN         1    455       L-serine dehydratase.
FT                                /FTId=PRO_0000171911.
SQ   SEQUENCE   455 AA;  48601 MW;  3FE9DD03EEC4A526 CRC64;
     MAISVFDLFS IGIGPSSSHT VGPMRAARMF ARRLRNEELL DSVASVRVEL YGSLGATGHG
     HGTPKAVLLG LEGDSPRTVD VESADDRVET IKSSGRISLL GDHEIAFAYD DDMVLHRRKA
     LPYHANGMTL WAYDAEGAEV LTKTYYSVGG GFVVDEDAVG ADRIVLDDTV LKYPFRTGDE
     LLRLARETGL SISALMLENE RAWRDEDEIR EGLLEIWRVM RACVDRGMTR EGILPGGLKV
     RRRAANTARK LRSEGDPQAL AMEWITLYAM AVNEENAAGG RVVTAPTNGA AGIIPAVLHY
     YMNFVPGADE DGVVRFLLAA GAIGMLFKEN ASISGAEVGC QGEVGSACSM AAGALAEVLG
     GSPEQVENAA EIGMEHNLGL TCDPVGGLVQ IPCIERNGMA AVKAVTAARM AMRGDGSHKV
     SLDKVIKTMK ETGADMSVKY KETARGGLAV NIIEC
//