ALR_VIBCH
ID ALR_VIBCH Reviewed; 361 AA.
AC Q9KUY6;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr1; OrderedLocusNames=VC_0372;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=24419381; DOI=10.1107/s1399004713024838;
RA Espaillat A., Carrasco-Lopez C., Bernardo-Garcia N., Pietrosemoli N.,
RA Otero L.H., Alvarez L., de Pedro M.A., Pazos F., Davis B.M., Waldor M.K.,
RA Hermoso J.A., Cava F.;
RT "Structural basis for the broad specificity of a new family of amino-acid
RT racemases.";
RL Acta Crystallogr. D 70:79-90(2014).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
CC Likely plays an important role in supplying D-alanine, which is an
CC indispensable constituent in the biosynthesis of bacterial cell-wall
CC peptidoglycan. To a lesser extent, is also able to racemize L-serine
CC and D-serine. Does not act on other proteinogenic amino-acids.
CC {ECO:0000269|PubMed:24419381}.
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:0000255|HAMAP-Rule:MF_01201,
CC ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:24419381};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for L-alanine {ECO:0000269|PubMed:24419381};
CC KM=17 mM for L-serine {ECO:0000269|PubMed:24419381};
CC Note=kcat is 1.42 sec(-1) with L-alanine as substrate. kcat is 1.16
CC sec(-1) with L-serine as substrate. {ECO:0000269|PubMed:24419381};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93545.1; ALT_INIT; Genomic_DNA.
DR PIR; H82329; H82329.
DR RefSeq; NP_230026.1; NC_002505.1.
DR RefSeq; WP_001913997.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KUY6; -.
DR SMR; Q9KUY6; -.
DR STRING; 243277.VC_0372; -.
DR DNASU; 2615051; -.
DR EnsemblBacteria; AAF93545; AAF93545; VC_0372.
DR GeneID; 57739108; -.
DR KEGG; vch:VC_0372; -.
DR PATRIC; fig|243277.26.peg.348; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_0_6; -.
DR OMA; ELMAVQH; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030378; F:serine racemase activity; IEA:RHEA.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_01201; Ala_racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR00492; alr; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 1: Evidence at protein level;
KW Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..361
FT /note="Alanine racemase"
FT /id="PRO_0000114591"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 254
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 361 AA; 39349 MW; EBD185735204A735 CRC64;
MKAATAYINL EALQHNLQRV KQQAPESKIM AVVKANGYGH GLRHIARHAL GADAFGVARI
EEALQLRASG VVKPILLLEG FYSPGDLPVL VTNNIQTVVH CEEQLQALEQ AQLETPVMVW
LKVDSGMHRL GVRPEQYQDF VARLHQCENV AKPLRYMSHF GCADELDKST TVEQTELFLS
LTQGCQGERS LAASAGLLAW PQSQLEWVRP GIIMYGVSPF VEKSAVQLGY QPVMTLKSHL
IAVREVKAGE SVGYGGTWTS QRDTKIGVIA IGYGDGYPRT APNGTPVVVN GRRVPIAGRV
SMDMLTVDLG PDACDRVGDE AMLWGNELPV EEVAAHIGTI GYELVTKLTS RVEMSYYGAG
V
