RACX_BACSU
ID RACX_BACSU Reviewed; 227 AA.
AC P32960;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Broad specificity amino-acid racemase RacX {ECO:0000305};
DE EC=5.1.1.10 {ECO:0000269|PubMed:28894939};
GN Name=racX; OrderedLocusNames=BSU34430;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8491712; DOI=10.1128/jb.175.10.2917-2925.1993;
RA Popham D.L., Setlow P.L.;
RT "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE
RT operon, which codes for penicillin-binding protein 4* and an apparent amino
RT acid racemase.";
RL J. Bacteriol. 175:2917-2925(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=28894939; DOI=10.1007/s00726-017-2486-2;
RA Miyamoto T., Katane M., Saitoh Y., Sekine M., Homma H.;
RT "Identification and characterization of novel broad-spectrum amino acid
RT racemases from Escherichia coli and Bacillus subtilis.";
RL Amino Acids 49:1885-1894(2017).
CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC substrates. Preferentially catalyzes the epimerization of LL-
CC diaminopimelate, as well as the racemization of D-lysine, L-arginine,
CC L-ornithine, L-lysine and D-arginine. Has lower activity against D-
CC ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L-
CC serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has
CC weak activity against L-norleucine, L-aminobutyric acid and L-
CC norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp,
CC Val, Leu, Ile, Trp, Cit and Aad) (PubMed:28894939). D-amino acids might
CC be used as components of peptidoglycan and/or be involved in
CC peptidoglycan metabolism and remodeling (PubMed:8491712,
CC PubMed:28894939). {ECO:0000269|PubMed:28894939,
CC ECO:0000269|PubMed:8491712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC EC=5.1.1.10; Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-
CC diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:57791; Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:32557; Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:32689;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine = D-ornithine; Xref=Rhea:RHEA:11584,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57668;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine = D-histidine; Xref=Rhea:RHEA:59188,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:142967;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine = D-tyrosine; Xref=Rhea:RHEA:59808,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58570;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine = D-phenylalanine; Xref=Rhea:RHEA:59804,
CC ChEBI:CHEBI:57981, ChEBI:CHEBI:58095;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine = D-glutamine; Xref=Rhea:RHEA:59276,
CC ChEBI:CHEBI:58000, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine = D-methionine; Xref=Rhea:RHEA:12492,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57932;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine = D-asparagine; Xref=Rhea:RHEA:59280,
CC ChEBI:CHEBI:58048, ChEBI:CHEBI:74337;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine = D-homoserine; Xref=Rhea:RHEA:59404,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:143081;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.9 mM for L-lysine {ECO:0000269|PubMed:28894939};
CC KM=69.3 mM for D-lysine {ECO:0000269|PubMed:28894939};
CC Vmax=2.99 nmol/min/mg enzyme with L-lysine as substrate
CC {ECO:0000269|PubMed:28894939};
CC Vmax=8.42 nmol/min/mg enzyme with D-lysine as substrate
CC {ECO:0000269|PubMed:28894939};
CC Note=kcat is 0.08 min(-1) with L-lysine as substrate. kcat is 0.224
CC min(-1) with D-lysine as substrate. {ECO:0000269|PubMed:28894939};
CC pH dependence:
CC Optimum pH is 8.5 with L-lysine as substrate.
CC {ECO:0000269|PubMed:28894939};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:28894939};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28894939}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed during vegetative growth and
CC significantly induced at the onset of sporulation.
CC {ECO:0000269|PubMed:8491712}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L10629; AAA22641.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z94043; CAB08017.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15448.1; -; Genomic_DNA.
DR PIR; B36908; B36908.
DR RefSeq; NP_391323.1; NC_000964.3.
DR RefSeq; WP_003244427.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P32960; -.
DR SMR; P32960; -.
DR STRING; 224308.BSU34430; -.
DR PaxDb; P32960; -.
DR EnsemblBacteria; CAB15448; CAB15448; BSU_34430.
DR GeneID; 938575; -.
DR KEGG; bsu:BSU34430; -.
DR PATRIC; fig|224308.179.peg.3730; -.
DR eggNOG; COG1794; Bacteria.
DR InParanoid; P32960; -.
DR OMA; SFIAMPC; -.
DR PhylomeDB; P32960; -.
DR BioCyc; BSUB:BSU34430-MON; -.
DR BRENDA; 5.1.1.10; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:RHEA.
DR GO; GO:0047679; F:arginine racemase activity; IEA:RHEA.
DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:RHEA.
DR GO; GO:0018113; F:lysine racemase activity; IEA:RHEA.
DR GO; GO:0018111; F:methionine racemase activity; IEA:RHEA.
DR GO; GO:0050157; F:ornithine racemase activity; IEA:RHEA.
DR GO; GO:0030378; F:serine racemase activity; IEA:RHEA.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR InterPro; IPR001920; Asp/Glu_race.
DR InterPro; IPR018187; Asp/Glu_racemase_AS_1.
DR InterPro; IPR033134; Asp/Glu_racemase_AS_2.
DR InterPro; IPR004380; Asp_race.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR SUPFAM; SSF53681; SSF53681; 2.
DR TIGRFAMs; TIGR00035; asp_race; 1.
DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE 1: Evidence at protein level;
KW Isomerase; Reference proteome; Sporulation.
FT CHAIN 1..227
FT /note="Broad specificity amino-acid racemase RacX"
FT /id="PRO_0000095536"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403"
FT ACT_SITE 191
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403"
FT BINDING 51..53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O58403"
FT BINDING 83..85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O58403"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O58403"
SQ SEQUENCE 227 AA; 25286 MW; B950A307C94B1D36 CRC64;
MIGILAGMGP KSTSPFIDKV IDYCQKLYGA SNDIDYPHMM IYSCPTPFYA DRPIDHDEMK
KAIIDGAVKL EKTGVDFIAL PCNTAHVYYE EIQQALSVPM LHIVEETIKE IPHPAKKAVV
LGTEPTIQSA IYQKVLKGNG QEVIHKDHWQ QAVNQLIAAI KQPNHMQHTQ ALWQTLYEEI
SQHADIIISA CTDLNAVLDH IQSEIPIIDS SACLAKSTVS TYLAYQS
