ID A0A1Q9Q647_9BACI Unreviewed; 220 AA.
AC A0A1Q9Q647;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=L-serine deaminase {ECO:0000256|PIRNR:PIRNR036692};
GN ORFNames=BTR25_01460 {ECO:0000313|EMBL:OLS42067.1};
OS Bacillus sp. MRMR6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1928617 {ECO:0000313|EMBL:OLS42067.1, ECO:0000313|Proteomes:UP000185615};
RN [1] {ECO:0000313|EMBL:OLS42067.1, ECO:0000313|Proteomes:UP000185615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRMR6 {ECO:0000313|EMBL:OLS42067.1,
RC ECO:0000313|Proteomes:UP000185615};
RA Thomas J.M., Ghebrendrias N., Rawat M.;
RT "Mendota Genome Annoucement.";
RL Submitted (DEC-2016) 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:OLS42067.1}.
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DR EMBL; MSLS01000001; OLS42067.1; -; Genomic_DNA.
DR RefSeq; WP_075685415.1; NZ_MSLS01000001.1.
DR AlphaFoldDB; A0A1Q9Q647; -.
DR STRING; 1928617.BTR25_01460; -.
DR OrthoDB; 9813137at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000185615; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000185615}.
FT DOMAIN 148..220
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 220 AA; 23990 MW; DB044468C9224737 CRC64;
MKYRSVFDII GPVMIGPSSS HTAGAARIGK VARSLFGREP KWANISLYGS FAKTYRGHGT
DVALVGGLLD FETDDVRIIN AIDIAKEKGI KLRFIEEDAV TDHPNTARVM IGDEKGELEL
VGISIGGGKI EVTELNGFEL KLSGNHPAIL VVHNDRFGAI ASVSNVLAKH EINIGHMEVS
RKEIGKIALM TIEVDQNIKE KILLELEKLP NILKVTKIVD
//
