ID K8E3T5_CARML Unreviewed; 221 AA.
AC K8E3T5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 2.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=L-serine deaminase {ECO:0000256|PIRNR:PIRNR036692};
GN Name=sdaAB {ECO:0000313|EMBL:CCO10909.2};
GN ORFNames=BN424_1468 {ECO:0000313|EMBL:CCO10909.2};
OS Carnobacterium maltaromaticum LMA28.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10909.2, ECO:0000313|Proteomes:UP000000212};
RN [1] {ECO:0000313|Proteomes:UP000000212}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
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}.
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DR EMBL; HE999757; CCO10909.2; -; Genomic_DNA.
DR RefSeq; WP_010049597.1; NC_019425.2.
DR AlphaFoldDB; K8E3T5; -.
DR STRING; 1234679.BN424_1468; -.
DR GeneID; 83606254; -.
DR KEGG; cml:BN424_1468; -.
DR eggNOG; COG1760; Bacteria.
DR HOGENOM; CLU_086592_0_0_9; -.
DR OrthoDB; 9813137at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000212; 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-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:UP000000212}.
FT DOMAIN 150..221
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 221 AA; 23889 MW; 4BB228083CC8ED83 CRC64;
MAQRYHSVFD IIGPVMVGPS SSHTAGAARI GKVVQKIFGA TPAKVDIFLY ESFAKTYRGH
GTDIALVGGL LGMDPADERL ADSIEIAKEL GIEINFIPTN EKAEHPNSVK LVVSTPEKSL
SVVGISIGGG KIQISEVNGF KIQLEENQPT FLIVHQDVPG MIAQVSNILA EKAINIGTMT
VSRESKGQQA IMMIEVDQYE VGETLAELKQ VEHIKQASFF K
//
