ID A0A0H2WNK9_SALPA Unreviewed; 356 AA.
AC A0A0H2WNK9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=dadX {ECO:0000313|EMBL:AAV77042.1};
GN OrderedLocusNames=SPA1071 {ECO:0000313|EMBL:AAV77042.1};
GN ORFNames=GNB70_002544 {ECO:0000313|EMBL:HAE6986847.1};
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319 {ECO:0000313|EMBL:AAV77042.1, ECO:0000313|Proteomes:UP000008185};
RN [1] {ECO:0000313|EMBL:AAV77042.1, ECO:0000313|Proteomes:UP000008185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 {ECO:0000313|EMBL:AAV77042.1}, and ATCC 9150 / SARB42
RC {ECO:0000313|Proteomes:UP000008185};
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
RN [2] {ECO:0000313|EMBL:HAE6986847.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 9150 {ECO:0000313|EMBL:HAE6986847.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:HAE6986847.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 9150 {ECO:0000313|EMBL:HAE6986847.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUL-2018) 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:0000256|HAMAP-Rule:MF_01201}.
CC -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to
CC pyruvate by DadA. {ECO:0000256|ARBA:ARBA00037715}.
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|ARBA:ARBA00000316, ECO:0000256|HAMAP-
CC 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.
CC {ECO:0000256|ARBA:ARBA00007880, ECO:0000256|HAMAP-Rule:MF_01201}.
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DR EMBL; CP000026; AAV77042.1; -; Genomic_DNA.
DR EMBL; DAASTS010000012; HAE6986847.1; -; Genomic_DNA.
DR RefSeq; WP_000197903.1; NC_006511.1.
DR AlphaFoldDB; A0A0H2WNK9; -.
DR SMR; A0A0H2WNK9; -.
DR KEGG; spt:SPA1071; -.
DR HOGENOM; CLU_028393_1_0_6; -.
DR OMA; LMAVQHI; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000008185; 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; cd06827; PLPDE_III_AR_proteobact; 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 3: Inferred from homology;
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}.
FT DOMAIN 232..356
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 35
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 253
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 35
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 356 AA; 38804 MW; 43DF23205EF25C69 CRC64;
MTRPIQASLD LQVMKQNLAI VRRAAPEARV WSVVKANAYG HGIERVWSAL GATDGFAMLN
LEEAITLRER GWKGPILMLE GFFHAQDLEA YDTYRLTTCI HSNWQLKALQ NARLNAPLDI
YVKVNSGMNR LGFQPERAQT VWQQLRAMRN VGEMTLMSHF AQADHPEGIG EAMRRIALAT
EGLQCAYSLS NSAATLWHPQ AHYDWVRPGI ILYGASPSGQ WRDIADTGLK PVMTLSSEII
GVQTLSAGER VGYGGGYSVT QEQRIGIVAA GYADGYPRHA PTGTPVLVDG IRTRTVGTVS
MDMLAVDLTP CPQAGIGTPV ELWGKEIKVD DVASAAGTLG YELLCAVAPR VPFVTT
//