ALGLR_THEMA
ID ALGLR_THEMA Reviewed; 379 AA.
AC Q9X0Z7; G4FE78; R4P0J4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
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};
GN OrderedLocusNames=TM_1270 {ECO:0000312|EMBL:AAD36345.1};
GN ORFNames=Tmari_1275 {ECO:0000312|EMBL:AGL50199.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
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 T.maritima lacks canonical alr and murI genes,
CC while D-alanine and D-glutamate are essential components of
CC peptidoglycan. Also displays a more efficient cystathionine beta-lyase
CC (CBL) activity, cleaving cystathionine to homocysteine and pyruvate;
CC however, this reaction seems not to be physiologically relevant since
CC T.maritima possesses an O-acetyl-homoserine thiolase (MetY) that
CC bypasses the need of CBL for methionine biosynthesis. Is not able to
CC produce cystathionine, using either O-acetylhomoserine or O-
CC succinylhomoserine, plus L-cysteine as substrates, and thus does not
CC possess cystathionine gamma-synthase (CGS) activity.
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=0.40 mM for cystathionine (at pH 8.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=0.70 mM for cystathionine (at pH 8.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=1.3 mM for cystathionine (at pH 8.0 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=4.2 mM for L-alanine (at pH 8.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=8.2 mM for L-alanine (at pH 8.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=0.38 mM for L-alanine (at pH 8.0 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=0.26 mM for L-glutamate (at pH 8.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC KM=1.4 mM for L-glutamate (at pH 8.0 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:28640457};
CC Note=kcat is 2.3 sec(-1) for cystathionine beta-lyase activity (at pH
CC 8.8 and 37 degrees Celsius). kcat is 3.3 sec(-1) for cystathionine
CC beta-lyase activity (at pH 8.0 and 37 degrees Celsius). kcat is 9.2
CC sec(-1) for cystathionine beta-lyase activity (at pH 8.0 and 70
CC degrees Celsius). kcat is 0.022 sec(-1) for alanine racemase activity
CC (at pH 8.8 and 37 degrees Celsius). kcat is 0.0065 sec(-1) for
CC alanine racemase activity (at pH 8.0 and 37 degrees Celsius). kcat is
CC 0.0024 sec(-1) for alanine racemase activity (at pH 8.0 and 70
CC degrees Celsius). kcat is 0.024 sec(-1) for glutamate racemase
CC activity (at pH 8.0 and 37 degrees Celsius). kcat is 1.0 sec(-1) for
CC glutamate racemase activity (at pH 8.0 and 70 degrees Celsius).
CC {ECO:0000269|PubMed:28640457};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius for the cystathionine beta-
CC lyase activity. {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; AE000512; AAD36345.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL50199.1; -; Genomic_DNA.
DR PIR; E72274; E72274.
DR RefSeq; NP_229075.1; NC_000853.1.
DR RefSeq; WP_004079973.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X0Z7; -.
DR SMR; Q9X0Z7; -.
DR STRING; 243274.THEMA_07985; -.
DR EnsemblBacteria; AAD36345; AAD36345; TM_1270.
DR EnsemblBacteria; AGL50199; AGL50199; Tmari_1275.
DR KEGG; tma:TM1270; -.
DR KEGG; tmm:Tmari_1275; -.
DR KEGG; tmw:THMA_1295; -.
DR PATRIC; fig|243274.17.peg.1273; -.
DR eggNOG; COG0626; Bacteria.
DR InParanoid; Q9X0Z7; -.
DR OMA; GPYTYGR; -.
DR OrthoDB; 637281at2; -.
DR BRENDA; 4.4.1.13; 6331.
DR BRENDA; 5.1.1.1; 6331.
DR BRENDA; 5.1.1.3; 6331.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:RHEA.
DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd00614; CGS_like; 1.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Cell shape; Isomerase; Lyase; Peptidoglycan synthesis; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..379
FT /note="L-alanine/L-glutamate racemase"
FT /id="PRO_0000448374"
FT BINDING 51..53
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 81..82
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 199..201
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 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P13254"
SQ SEQUENCE 379 AA; 42753 MW; E522AACAC3DDBD7A CRC64;
MNTDDILFSY GEEDIPLKAL SFPIFETTNF YFDSFDEMSK ALRNGDYEFV YKRGSNPTTR
LVEKKLAALE ECEDARLVAS GMSAISLSIL HFLSSGDHVV CVDEAYSWAK KFFNYLSKKF
DIEVSYVPPD AERIVEAITK KTKLIYLESP TSMRMKVIDI RKVTEAAGEL KIKTVIDNTW
ASPIFQKPKL LGVDVVVHSA TKYISGHGDV MAGVIAGDVE DMKNIFVDEY KNIGPVLSPI
EAWLILRGLR TLELRMKKHY ENALVVSDFL MDHPKVLEVN YPMNPRSPQY ELASSQMSGG
SGLMSFRLKT DSAEKVKEFV ESLRVFRMAV SWGSHENLVV PRVAYGDCPK KDVNLIRIHV
GLGDPEKLVE DLDQALKKI
