ALR_CARHZ
ID ALR_CARHZ Reviewed; 368 AA.
AC Q9F8I0; Q3AEB2;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
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=CHY_0667;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-329.
RA Gonzalez J.M., Robb F.T.;
RT "A genomic survey of the extreme thermophilic, CO-utilizing bacterium
RT Carboxydothermus hydrogenoformans.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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; CP000141; ABB13915.1; -; Genomic_DNA.
DR EMBL; AF244653; AAG23602.1; -; Genomic_DNA.
DR RefSeq; WP_011343598.1; NC_007503.1.
DR AlphaFoldDB; Q9F8I0; -.
DR SMR; Q9F8I0; -.
DR STRING; 246194.CHY_0667; -.
DR PRIDE; Q9F8I0; -.
DR EnsemblBacteria; ABB13915; ABB13915; CHY_0667.
DR KEGG; chy:CHY_0667; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_9; -.
DR OMA; HMTHFSD; -.
DR OrthoDB; 859043at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000002706; 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..368
FT /note="Alanine racemase"
FT /id="PRO_0000114506"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 261
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 309
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"
FT CONFLICT 98..103
FT /note="PTLHHR -> AGRTGP (in Ref. 2; AAG23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="A -> T (in Ref. 2; AAG23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..316
FT /note="AV -> RW (in Ref. 2; AAG23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="N -> L (in Ref. 2; AAG23602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41632 MW; 0FA978BE431D3E38 CRC64;
MRPVWAEVNL ENIRHNFREV KRLARQAEAM PVIKANAYGH GAVEVAKALI AEGAKRFAVA
ILDEGIKLRE AGIDAPVLIL GYTPPEEVEK LLFYNLTPTL HHRELALAYQ ERLERLKKTL
FYHLKIDTGM GRIGFWYEEL EKIEEVLKLK NLEAEGVYTH FARADEQDLS FSKLQIERFN
IVLKHLKAKG IEVKYRHAAN SAAIMRLPEA HYDLVRPGIM LYGEYPSRDV PRELAHLKPA
LTLKARVSQV KKVPAGFTVS YGSTYVTSKA TLIVSLPLGY ADGYFRRLSN RGVVLINGKR
WSIAGRVCMD QLMVAVDETE RVNPGDEAVL LGKQGEETIT AMEMADLVGT INYEILTNIS
YRVPRIYV
