ID E2ZED2_9FIRM Unreviewed; 222 AA.
AC E2ZED2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=L-serine deaminase {ECO:0000256|PIRNR:PIRNR036692};
GN Name=sdaAB {ECO:0000313|EMBL:EFQ08450.1};
GN ORFNames=HMPREF9436_00006 {ECO:0000313|EMBL:EFQ08450.1};
OS Faecalibacterium cf. prausnitzii KLE1255.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ08450.1, ECO:0000313|Proteomes:UP000006028};
RN [1] {ECO:0000313|EMBL:EFQ08450.1, ECO:0000313|Proteomes:UP000006028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ08450.1,
RC ECO:0000313|Proteomes:UP000006028};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFQ08450.1}.
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DR EMBL; AECU01000002; EFQ08450.1; -; Genomic_DNA.
DR RefSeq; WP_005936832.1; NZ_GL538214.1.
DR AlphaFoldDB; E2ZED2; -.
DR STRING; 748224.HMPREF9436_00006; -.
DR eggNOG; COG1760; Bacteria.
DR HOGENOM; CLU_086592_0_0_9; -.
DR OrthoDB; 9813137at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006028; 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 150..222
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 222 AA; 24136 MW; 14489C1B6D280447 CRC64;
MAFISVFDVL GPNMIGPSSS HTAGAEIIAF LAQKMIAPPL KRADFTLYGS FAKTYHGHGT
DRALLGGIMG FSADDTRIRD SFAIATDRGL GYSFTPNEVE TDIHPNTVDI RMENAAGQVM
TVRGESLGGG KVRIVRINGV EVDFTGEYNA LIVVQKDKPG VVAHITKILS DRSVNIAFMR
LFREEKGHTA YTIVESDERL PEGVDQLLLA NPNINDVMVV QP
//
