ALR_CAMJE
ID ALR_CAMJE Reviewed; 328 AA.
AC Q9PP26; Q0P9Z3;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=alr; OrderedLocusNames=Cj0905c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000255|HAMAP-Rule:MF_01201}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
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}.
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DR EMBL; AL111168; CAL35026.1; -; Genomic_DNA.
DR PIR; A81364; A81364.
DR RefSeq; WP_002852617.1; NC_002163.1.
DR RefSeq; YP_002344304.1; NC_002163.1.
DR AlphaFoldDB; Q9PP26; -.
DR SMR; Q9PP26; -.
DR IntAct; Q9PP26; 11.
DR STRING; 192222.Cj0905c; -.
DR PaxDb; Q9PP26; -.
DR PRIDE; Q9PP26; -.
DR EnsemblBacteria; CAL35026; CAL35026; Cj0905c.
DR GeneID; 905209; -.
DR KEGG; cje:Cj0905c; -.
DR PATRIC; fig|192222.6.peg.889; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_7; -.
DR OMA; TSMNTVM; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..328
FT /note="Alanine racemase"
FT /id="PRO_0000114505"
FT ACT_SITE 33
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 237
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 33
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 328 AA; 37256 MW; 1F82682833905D22 CRC64;
MSLIKIDQKA YEYNLRHIAK KIGSFQRLIC VFKDNAYGHG AKLLAPLAKN LGVSFVAVKS
EEEAREIEEF FENILILSHR PHGNENSRFI YALNDISQVK NYKQDIKIHL KIDTGMHRNG
ICVENLEHAI NLIQGSDLKL TGMFTHFASA DEMDGSFFVQ KENFQKAKKI VKKYFSNLLF
HSYNSAALFR GKIPEDEYCR VGLVQFGYGD SNLKRVLSLY AHRLSQRILQ KGQSIGYGGI
FTAAKDMEVA TYDLGYADGL FRYNGRGELV LGNGKAMLGK MSMDSFSCEN SGEEICVFKD
ADIWADFFHT INYEILVKLN PNIQRVLV
