ALGLR_WOLPM
ID ALGLR_WOLPM Reviewed; 403 AA.
AC Q73GL9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=L-alanine/L-glutamate racemase {ECO:0000305|PubMed:28640457};
DE EC=5.1.1.1 {ECO:0000269|PubMed:28640457};
DE EC=5.1.1.3 {ECO:0000269|PubMed:28640457};
GN Name=aar {ECO:0000303|PubMed:28640457};
GN Synonyms=metC {ECO:0000303|PubMed:28640457, ECO:0000312|EMBL:AAS14597.1};
GN OrderedLocusNames=WD_0925 {ECO:0000312|EMBL:AAS14597.1};
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RX PubMed=28640457; DOI=10.1111/mmi.13737;
RA Ferla M.P., Brewster J.L., Hall K.R., Evans G.B., Patrick W.M.;
RT "Primordial-like enzymes from bacteria with reduced genomes.";
RL Mol. Microbiol. 105:508-524(2017).
CC -!- FUNCTION: Catalyzes the racemization of L-alanine to D-alanine, and of
CC L-glutamate to D-glutamate. The activity is low, but likely
CC physiological since W.pipientis wMel lacks canonical alr and murI
CC genes, while D-alanine and D-glutamate are essential components of
CC peptidoglycan. Also displays a vestigial cystathionine beta-lyase (CBL)
CC activity, cleaving cystathionine to homocysteine and pyruvate; however,
CC this reaction seems not to be physiologically relevant since the only
CC met gene in the genome of this obligately intracellular parasitic
CC bacterium is metC, demonstrating that it is a methionine auxotroph.
CC {ECO:0000269|PubMed:28640457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC Evidence={ECO:0000269|PubMed:28640457};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20250;
CC Evidence={ECO:0000305|PubMed:28640457};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3;
CC Evidence={ECO:0000269|PubMed:28640457};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12814;
CC Evidence={ECO:0000305|PubMed:28640457};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000269|PubMed:28640457};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P13254};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.02 mM for cystathionine (at pH 8.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=3.8 mM for L-alanine (at pH 8.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=0.80 mM for L-glutamate (at pH 8.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC Note=kcat is 0.001 sec(-1) for cystathionine beta-lyase activity (at
CC pH 8.8 and 37 degrees Celsius). kcat is 2.3 sec(-1) for alanine
CC racemase activity (at pH 8.8 and 37 degrees Celsius). kcat is 0.017
CC sec(-1) for glutamate racemase activity (at pH 8.0 and 37 degrees
CC Celsius). {ECO:0000269|PubMed:28640457};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000305|PubMed:28640457}.
CC -!- SUBUNIT: Homotetramer; dimer of active dimers.
CC {ECO:0000250|UniProtKB:P13254}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AE017196; AAS14597.1; -; Genomic_DNA.
DR RefSeq; WP_010962928.1; NC_002978.6.
DR AlphaFoldDB; Q73GL9; -.
DR SMR; Q73GL9; -.
DR STRING; 163164.WD_0925; -.
DR EnsemblBacteria; AAS14597; AAS14597; WD_0925.
DR GeneID; 29554913; -.
DR KEGG; wol:WD_0925; -.
DR eggNOG; COG0626; Bacteria.
DR OMA; GPYTYGR; -.
DR OrthoDB; 637281at2; -.
DR BRENDA; 4.4.1.13; 17708.
DR BRENDA; 5.1.1.1; 17708.
DR BRENDA; 5.1.1.3; 17708.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008215; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006233; Cys_b_lyase_bac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43500; PTHR43500; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01324; cysta_beta_ly_B; 1.
PE 1: Evidence at protein level;
KW Cell shape; Isomerase; Lyase; Peptidoglycan synthesis; Pyridoxal phosphate.
FT CHAIN 1..403
FT /note="L-alanine/L-glutamate racemase"
FT /id="PRO_0000448375"
FT BINDING 62..64
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 92..93
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 209..211
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P13254"
SQ SEQUENCE 403 AA; 45238 MW; E9EB5D43D747D086 CRC64;
MKEESILVKA GRKFNDYKGS MNPPVYHSST ILFPTYKDYL NAANGESIYD VINDGVARDY
SYSNVGTPTV HYLSNALAEI EGSGQALIYP SGLFALTFAI LTFAKAGSHV LIQDNSYYRL
RRFAENELPK RGTEVTFYDP TQDITDLIQS NTSLIMIETP GSVTFEISNI EHIVKVAKEH
KIVTVCDNSW ATPLLFKPLD YGVDVALYAV TKYLAGHSDL VMGAIIAEGE IFKLLYESYK
NYGVTIQSHD CYLAHRGLRT LYTRMKRHQN TAMEVAKWLE KHSKIKKVLY PALPFHPQHE
LWKSYFKGAS GTFSIALDRE YSCEELSCMV DHMKIFGIGA SWGGCDSLIL PIDRRSMSRS
VMNSDYGGSF IRIFCGLEDP EDLISDLNAA LARLPCLNTK TGR
