ID   C0ZY44_RHOE4            Unreviewed;       452 AA.
AC   C0ZY44;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=L-serine dehydratase {ECO:0000256|RuleBase:RU366059};
DE            EC=4.3.1.17 {ECO:0000256|RuleBase:RU366059};
GN   Name=sdaA {ECO:0000313|EMBL:BAH33279.1};
GN   OrderedLocusNames=RER_25710 {ECO:0000313|EMBL:BAH33279.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH33279.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH33279.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT   strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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         Evidence={ECO:0000256|ARBA:ARBA00001161,
CC         ECO:0000256|RuleBase:RU366059};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU366059};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC       family. {ECO:0000256|ARBA:ARBA00008636, ECO:0000256|RuleBase:RU366059}.
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DR   EMBL; AP008957; BAH33279.1; -; Genomic_DNA.
DR   RefSeq; WP_020907391.1; NC_012490.1.
DR   AlphaFoldDB; C0ZY44; -.
DR   KEGG; rer:RER_25710; -.
DR   PATRIC; fig|234621.6.peg.3059; -.
DR   eggNOG; COG1760; Bacteria.
DR   HOGENOM; CLU_022305_0_1_11; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR004644; Fe-S_L-Ser_mono.
DR   InterPro; IPR005130; Ser_deHydtase-like_asu.
DR   InterPro; IPR005131; Ser_deHydtase_bsu.
DR   NCBIfam; TIGR00720; sda_mono; 1.
DR   PANTHER; PTHR30182; L-SERINE DEHYDRATASE; 1.
DR   PANTHER; PTHR30182:SF1; L-SERINE DEHYDRATASE 1; 1.
DR   Pfam; PF03313; SDH_alpha; 1.
DR   Pfam; PF03315; SDH_beta; 1.
DR   SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU366059};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW   ECO:0000256|RuleBase:RU366059};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU366059};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU366059};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU366059};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366059}.
FT   DOMAIN          9..161
FT                   /note="Serine dehydratase beta chain"
FT                   /evidence="ECO:0000259|Pfam:PF03315"
FT   DOMAIN          191..446
FT                   /note="Serine dehydratase-like alpha subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03313"
SQ   SEQUENCE   452 AA;  46924 MW;  4502136C585177A0 CRC64;
     MSTTGVYVSA LEFFSIGIGP SSSHTVGPMR AAHTFGGELS AAGLTASVDR IRCNLHGSLA
     ATGIGHCTPD AVIAGLRGLD PETCEPTDVH GRWAELSDGG SVMLVGGSLG HVVFTHEDMV
     FEPLVRRHGH PNSMTLTAFS GREIVCTSTY LSIGGGFVLR AGTETQASAH SINSRYRTAK
     ELLAECDSGT IAELALSDEI AMHGKDRAFT GIDAIWSAMR ACIERGTQTE GVLPGRLGVR
     RRARSANIQL EQRNCDPFSR EWLTVYAMAV NEENAAGGRV VTAPTNGAAG IVPAVLYHHI
     RATGAGAHDV RTFLLTAAAI GSIIKANASI SGAEAGCQGE VGAACAMAAA GLCAVMGGSP
     RQIENAAEIA MEHHLGLTCD PVGGLVQIPC IERNAVAAST AVTAAQLAYL GDGTHVVSLD
     TVIETMRQTG NDMSVRYKET SEGGLAVNVV EC
//