ID Q180W0_CLOD6 Unreviewed; 385 AA.
AC Q180W0;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr2 {ECO:0000313|EMBL:CAJ70366.1};
GN OrderedLocusNames=CD630_34630 {ECO:0000313|EMBL:CAJ70366.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ70366.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ70366.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ70366.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2] {ECO:0007829|PDB:4LUS, ECO:0007829|PDB:4LUT}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RX PubMed=25004969; DOI=10.1107/S1399004714009419;
RA Asojo O.A., Nelson S.K., Mootien S., Lee Y., Rezende W.C., Hyman D.A.,
RA Matsumoto M.M., Reiling S., Kelleher A., Ledizet M., Koski R.A.,
RA Anthony K.G.;
RT "Structural and biochemical analyses of alanine racemase from the
RT multidrug-resistant Clostridium difficile strain 630.";
RL Acta Crystallogr. D 70:1922-1933(2014).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; AM180355; CAJ70366.1; -; Genomic_DNA.
DR RefSeq; WP_003437830.1; NZ_JAUPES010000009.1.
DR RefSeq; YP_001089983.1; NC_009089.1.
DR PDB; 4LUS; X-ray; 2.10 A; A/B/C/D=1-385.
DR PDB; 4LUT; X-ray; 2.26 A; A/B=1-385.
DR PDB; 4LUY; X-ray; 2.60 A; A/B=1-385.
DR PDBsum; 4LUS; -.
DR PDBsum; 4LUT; -.
DR PDBsum; 4LUY; -.
DR AlphaFoldDB; Q180W0; -.
DR SMR; Q180W0; -.
DR STRING; 272563.CD630_34630; -.
DR EnsemblBacteria; CAJ70366; CAJ70366; CD630_34630.
DR KEGG; cdf:CD630_34630; -.
DR KEGG; pdc:CDIF630_03774; -.
DR PATRIC; fig|272563.120.peg.3660; -.
DR eggNOG; COG0787; Bacteria.
DR OrthoDB; 9813814at2; -.
DR PhylomeDB; Q180W0; -.
DR BioCyc; PDIF272563:G12WB-3643-MONOMER; -.
DR BRENDA; 5.1.1.1; 1473.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001978; 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 CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4LUS, ECO:0007829|PDB:4LUT};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000001978}.
FT DOMAIN 247..371
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 268
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 385 AA; 43310 MW; C164196EB29029D7 CRC64;
MQKITVPTWA EINLDNLRFN LNNIKNLLEE DIKICGVIKA DAYGHGAVEV AKLLEKEKVD
YLAVARTAEG IELRQNGITL PILNLGYTPD EAFEDSIKNK ITMTVYSLET AQKINEIAKS
LGEKACVHVK IDSGMTRIGF QPNEESVQEI IELNKLEYID LEGMFTHFAT ADEVSKEYTY
KQANNYKFMS DKLDEAGVKI AIKHVSNSAA IMDCPDLRLN MVRAGIILYG HYPSDDVFKD
RLELRPAMKL KSKIGHIKQV EPGVGISYGL KYTTTGKETI ATVPIGYADG FTRIQKNPKV
LIKGEVFDVV GRICMDQIMV RIDKDIDIKV GDEVILFGEG EVTAERIAKD LGTINYEVLC
MISRRVDRVY MENNELVQIN SYLLK
//
