S1544_SULMK
ID S1544_SULMK Reviewed; 392 AA.
AC P0DV65;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=L-serine phosphate decarboxylase {ECO:0000305};
DE EC=4.1.1.- {ECO:0000269|PubMed:31325159};
DE AltName: Full=CobD homolog SMUL_1544 {ECO:0000303|PubMed:31325159};
DE Short=SmCobD {ECO:0000303|PubMed:31325159};
DE AltName: Full=L-serine O-phosphate decarboxylase {ECO:0000303|PubMed:31325159};
DE Short=L-Ser-P decarboxylase {ECO:0000303|PubMed:27274028, ECO:0000303|PubMed:31325159};
DE AltName: Full=Norcobamide biosynthesis protein SMUL_1544 {ECO:0000303|PubMed:27274028};
DE AltName: Full=Threonine phosphate decarboxylase-like enzyme {ECO:0000312|EMBL:AHJ12804.1};
GN ORFNames=SMUL_1544 {ECO:0000303|PubMed:27274028,
GN ECO:0000303|PubMed:31325159, ECO:0000312|EMBL:AHJ12804.1};
OS Sulfurospirillum multivorans (strain DM 12446 / JCM 15788 / NBRC 109480).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurospirillaceae; Sulfurospirillum.
OX NCBI_TaxID=1150621;
RN [1] {ECO:0000312|EMBL:AHJ12804.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM 12446 / JCM 15788 / NBRC 109480 {ECO:0000312|EMBL:AHJ12804.1};
RX PubMed=25186071; DOI=10.1111/1462-2920.12589;
RA Goris T., Schubert T., Gadkari J., Wubet T., Tarkka M., Buscot F.,
RA Adrian L., Diekert G.;
RT "Insights into organohalide respiration and the versatile catabolism of
RT Sulfurospirillum multivorans gained from comparative genomics and
RT physiological studies.";
RL Environ. Microbiol. 16:3562-3580(2014).
RN [2]
RP FUNCTION.
RC STRAIN=DM 12446 / JCM 15788 / NBRC 109480 {ECO:0000303|PubMed:27274028};
RX PubMed=27274028; DOI=10.1128/jb.00289-16;
RA Keller S., Treder A., von Reuss S.H., Escalante-Semerena J.C., Schubert T.;
RT "The SMUL_1544 Gene Product Governs Norcobamide Biosynthesis in the
RT Tetrachloroethene-Respiring Bacterium Sulfurospirillum multivorans.";
RL J. Bacteriol. 198:2236-2243(2016).
RN [3] {ECO:0007744|PDB:6OUX}
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 2-392, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, PATHWAY, SUBUNIT, REGION, MUTAGENESIS OF 2-VAL--ASN-6;
RP 2-VAL--GLN-11; 2-VAL--PHE-16; 2-VAL--GLN-21; 2-VAL--SER-29; HIS-26 AND
RP SER-242, AND PHYLOGENETIC ANALYSIS.
RC STRAIN=DM 12446 / JCM 15788 / NBRC 109480 {ECO:0000303|PubMed:31325159};
RX PubMed=31325159; DOI=10.1002/1873-3468.13543;
RA Keller S., Wetterhorn K.M., Vecellio A., Seeger M., Rayment I.,
RA Schubert T.;
RT "Structural and functional analysis of an l-serine O-phosphate
RT decarboxylase involved in norcobamide biosynthesis.";
RL FEBS Lett. 593:3040-3053(2019).
CC -!- FUNCTION: Pyridoxal phosphate (PLP)-dependent decarboxylase involved in
CC the biosynthesis of norcobamides, cofactors in the tetrachloroethene
CC reductive dehalogenase PceA of S.multivorans. Catalyzes the
CC decarboxylation of L-serine O-phosphate to ethanolamine O-phosphate,
CC the precursor for the linkage between the nucleotide loop and the
CC corrin ring in norcobamide. Less active with L-threonine phosphate. No
CC activity with L-serine or L-threonine. Has no aminotransferase activity
CC as no production of L-glutamate with L-histidinol phosphate and 2-
CC oxoglutarate as substrates (PubMed:31325159). Complements growth
CC defects in the S.enterica cobD deletion mutant, but of the cobamides,
CC the norpseudo-vitamin B12 (norpseudo-B12) rather than the pseudo-B12 is
CC produced in the mutant. However, addition of L-threonine phosphate to
CC the culture minimal medium of the mutant results in formation of also
CC the pseudo-B12, indicating the dual substrate specificity of this
CC enzyme (PubMed:27274028). {ECO:0000269|PubMed:27274028,
CC ECO:0000269|PubMed:31325159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + O-phospho-L-serine = CO2 + phosphoethanolamine;
CC Xref=Rhea:RHEA:69548, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57524, ChEBI:CHEBI:58190;
CC Evidence={ECO:0000269|PubMed:31325159};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:31325159};
CC -!- PATHWAY: Cofactor biosynthesis. {ECO:0000305|PubMed:31325159}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31325159}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CP007201; AHJ12804.1; -; Genomic_DNA.
DR PDB; 6OUX; X-ray; 1.94 A; A/B=2-392.
DR PDBsum; 6OUX; -.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..392
FT /note="L-serine phosphate decarboxylase"
FT /id="PRO_0000455391"
FT REGION 22..29
FT /note="Required for catalytic activity"
FT /evidence="ECO:0000269|PubMed:31325159"
FT BINDING 180
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT BINDING 354
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT BINDING 368
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT MUTAGEN 2..29
FT /note="Missing: Loss of enzyme activity with L-serine
FT phosphate and with L-threonine phosphate. No effect in
FT pyridoxal phosphate (PLP)-binding."
FT /evidence="ECO:0000269|PubMed:31325159"
FT MUTAGEN 2..21
FT /note="Missing: Decreased enzyme activity by about 30%
FT compared to wild-type with L-serine phosphate. No effect on
FT enzyme activity with L-threonine phosphate."
FT /evidence="ECO:0000269|PubMed:31325159"
FT MUTAGEN 2..16
FT /note="Missing: Decreased enzyme activity by about 30%
FT compared to wild-type with L-serine phosphate. No effect on
FT enzyme activity with L-threonine phosphate."
FT /evidence="ECO:0000269|PubMed:31325159"
FT MUTAGEN 2..11
FT /note="Missing: Decreased enzyme activity by about 30%
FT compared to wild-type with L-serine phosphate. No effect on
FT enzyme activity with L-threonine phosphate."
FT /evidence="ECO:0000269|PubMed:31325159"
FT MUTAGEN 2..6
FT /note="Missing: No effect on enzyme activity with L-serine
FT phosphate or with L-threonine phosphate."
FT /evidence="ECO:0000269|PubMed:31325159"
FT MUTAGEN 26
FT /note="H->A: Significantly decreased enzyme activity. No
FT effect in pyridoxal phosphate (PLP)-binding."
FT /evidence="ECO:0000269|PubMed:31325159"
FT MUTAGEN 242
FT /note="S->T: Increased enzyme activity with of L-threonine
FT phosphate and a decreased activity with L-serine phosphate.
FT Exhibits similar activity rates with both substrates."
FT /evidence="ECO:0000269|PubMed:31325159"
SQ SEQUENCE 392 AA; 45043 MW; 50EDA19546466057 CRC64;
MVDTMNARNT QFTKAFHALK QNAGSHSPSM EDLKKMFPTL EIKIDACYLS NPYASELVLD
YIDRELIQTN AYKKVLTHYP SQQRSLQKVM AESLHVKPEN IFIGNGATEI IQMLLQQEEV
QKVALMIPTF SSYYEFVGKG CEVVYFPLNE RDDYSFDADK YCQFIENEQP DTVVLINPNN
PNGAYLSLEK MHILLKRLAF VPRIIIDESF IHFAYEDEAL TCLSSTVLFD MYPNVIIVKS
LSKDFGIAGV RLGYALMDSR KIDALLEHGF LWNINGIGEY CLRLFVREDF LKRYEEARKQ
YIKEMCRFKE ALLGIENVYV YPSMANFVML KLPSRIKASF VISALLVEYG IYVRTMADKI
GVEGECIRIA GRTREENNCI VMALKSILKD SK
