ID W5Y602_9CORY Unreviewed; 365 AA.
AC W5Y602;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 28-FEB-2018, entry version 26.
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=alr {ECO:0000313|EMBL:AHI21903.1};
GN ORFNames=B843_02560 {ECO:0000313|EMBL:AHI21903.1};
OS Corynebacterium vitaeruminis DSM 20294.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI21903.1, ECO:0000313|Proteomes:UP000019222};
RN [1] {ECO:0000313|EMBL:AHI21903.1, ECO:0000313|Proteomes:UP000019222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium vitaeruminis DSM
RT 20294.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
CC -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC ECO:0000256|PIRSR:PIRSR600821-50,
CC ECO:0000256|SAAS:SAAS00758845};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|HAMAP-Rule:MF_01201}.
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DR EMBL; CP004353; AHI21903.1; -; Genomic_DNA.
DR RefSeq; WP_025251961.1; NZ_CP004353.1.
DR EnsemblBacteria; AHI21903; AHI21903; B843_02560.
DR KEGG; cvt:B843_02560; -.
DR PATRIC; fig|1224164.3.peg.504; -.
DR KO; K01775; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000019222; 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; -; 2.
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; 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.
PE 3: Inferred from homology;
KW Complete proteome {ECO:0000313|Proteomes:UP000019222};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AHI21903.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW Reference proteome {ECO:0000313|Proteomes:UP000019222}.
FT DOMAIN 238 364 Ala_racemase_C. {ECO:0000259|SMART:
FT SM01005}.
FT ACT_SITE 34 34 Proton acceptor; specific for D-alanine.
FT {ECO:0000256|HAMAP-Rule:MF_01201}.
FT ACT_SITE 259 259 Proton acceptor; specific for L-alanine.
FT {ECO:0000256|HAMAP-Rule:MF_01201}.
FT BINDING 132 132 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT 52}.
FT BINDING 307 307 Substrate; via amide nitrogen.
FT {ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52}.
FT MOD_RES 34 34 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50}.
SQ SEQUENCE 365 AA; 39378 MW; A318BF82711A9CC2 CRC64;
MNLLETRIDL DAIAFNTRKI KELVAPAQLM CVVKADAYNH GAAQAARVMS ENGADQFGVA
TLAEALELRE AGITLPILCW IWSPEQKELA RKAVAAGVDL AVVSTAHADF LAELGKEHPV
RVTVKVDTGL HRSGVDEASW AEVFALLRDA QGIEVTGIFS HLACADEPGN PYTDFQADNF
RRAIELGRSL GLALPVNHLS NSPATLTRPD LRFDMVRPGI ALYGLEPIPE QDHGLREAMS
WVGKVTVVKP VKASEGTSYS MTWHAERDGY LAVVPAGYAD GVPRAAQGHI RVTIGGRQYP
QVGRVCMDQF VIDLGENPHA VAPGDEAVIF GPDGMSATEL AQGIGTINYE VICRPTGRTR
RVTKP
//
