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Database: UniProt
Entry: W1TRT0_9FIRM
LinkDB: W1TRT0_9FIRM
Original site: W1TRT0_9FIRM 
ID   W1TRT0_9FIRM            Unreviewed;       219 AA.
AC   W1TRT0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=L-serine deaminase {ECO:0000256|PIRNR:PIRNR036692};
GN   ORFNames=Q612_NSC00356G0002 {ECO:0000313|EMBL:ETI84337.1};
OS   Negativicoccus succinicivorans DORA_17_25.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Negativicoccus.
OX   NCBI_TaxID=1403945 {ECO:0000313|EMBL:ETI84337.1, ECO:0000313|Proteomes:UP000018840};
RN   [1] {ECO:0000313|EMBL:ETI84337.1, ECO:0000313|Proteomes:UP000018840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DORA_17_25 {ECO:0000313|Proteomes:UP000018840};
RA   Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA   Banfield J.F.;
RT   "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT   community with otherwise low bacterial novelty that shifts toward anaerobic
RT   metabolism during the third week of life.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR036692, 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, ECO:0000256|PIRNR:PIRNR036692}.
CC   -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC       family. {ECO:0000256|ARBA:ARBA00008636, ECO:0000256|PIRNR:PIRNR036692,
CC       ECO:0000256|RuleBase:RU366059}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETI84337.1}.
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DR   EMBL; AZMC01000356; ETI84337.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1TRT0; -.
DR   PATRIC; fig|1403945.3.peg.1408; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000018840; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd04903; ACT_LSD; 1.
DR   Gene3D; 3.30.70.260; -; 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   NCBIfam; TIGR00719; sda_beta; 1.
DR   PANTHER; PTHR30182; L-SERINE DEHYDRATASE; 1.
DR   PANTHER; PTHR30182:SF12; L-SERINE DEHYDRATASE, BETA CHAIN-RELATED; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF03315; SDH_beta; 1.
DR   PIRSF; PIRSF036692; SDH_B; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR036692, ECO:0000256|RuleBase:RU366059};
KW   Gluconeogenesis {ECO:0000256|PIRNR:PIRNR036692,
KW   ECO:0000256|RuleBase:RU366059};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR036692};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR036692};
KW   Lyase {ECO:0000256|PIRNR:PIRNR036692, ECO:0000256|RuleBase:RU366059};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR036692}.
FT   DOMAIN          146..218
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   219 AA;  23703 MW;  16EC0429B1ED8F05 CRC64;
     MGVFDIIGPV MIGPSSSHTA GAARLGRLAR YLLGESPIKA DITFYGSFAQ TYRGHGTDRA
     CVAGLLNWAP DDQRLRDALT MAPELGLQVT ITASAAETEH PNTVRFHLTG SSGKARELMG
     VSTGGGRIRM REFDGYSVDL DGSNHTLLTR HNDRPGIVAF VSQILAAQDI NISAMRLFRQ
     ERKRLAMMFI ETDTPVANAT LAEIAAHPAI EVVRTFPPV
//
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