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Database: UniProt/TrEMBL
Entry: W5WSF9_9CORY
LinkDB: W5WSF9_9CORY
Original site: W5WSF9_9CORY 
ID   W5WSF9_9CORY            Unreviewed;       588 AA.
AC   W5WSF9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-SEP-2017, entry version 28.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=CFAL_09520 {ECO:0000313|EMBL:AHI03818.1};
OS   Corynebacterium falsenii DSM 44353.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1451189 {ECO:0000313|EMBL:AHI03818.1, ECO:0000313|Proteomes:UP000019232};
RN   [1] {ECO:0000313|EMBL:AHI03818.1, ECO:0000313|Proteomes:UP000019232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL 8171 {ECO:0000313|EMBL:AHI03818.1};
RX   PubMed=24604654;
RA   Glaub A., Bomholt C., Gravermann K., Brinkrolf K., Albersmeier A.,
RA   Ruckert C., Tauch A.;
RT   "Complete Genome Sequence of Corynebacterium falsenii DSM 44353 To
RT   Study the Evolution of Corynebacterium Cluster 3 Species.";
RL   Genome Announc. 2:e00158-14(2014).
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; CP007156; AHI03818.1; -; Genomic_DNA.
DR   RefSeq; WP_052337585.1; NZ_CP007156.1.
DR   EnsemblBacteria; AHI03818; AHI03818; CFAL_09520.
DR   KEGG; cfn:CFAL_09520; -.
DR   PATRIC; fig|1451189.3.peg.1866; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000019232; 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   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF02367; TsaE; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019232};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
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:UP000019232}.
FT   DOMAIN      248    380       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     38     38       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    269    269       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     139    139       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     317    317       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      38     38       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   588 AA;  61863 MW;  3801EC7A611FB1D6 CRC64;
     MDSEIHLAEL VVDLGAIAHN VQELVAAATP AEVMAVVKAD GYNHGLREVV DTVIAAGATH
     LGVATVGEAL AVRAAGGAGA TAPVTAWMWF PGEDLSAALA QNITIGIPSL AHAESLIEQA
     GSGAGPVPAT LMVDTGLSRS GVSPAEWEST VELLAQHTDL VDVRGLMSHL ATADTPNADP
     ATDMQAQRFH RAIEFCRARG LDVPCNHLAN TPATLTRPDT HHEMVRPGVG IYGVDPVEPK
     AGATFRPAMT FRARVITTRV VAAGEAVSYG HTWRAEVDTR TAVVAVGYAD GIPRSASGRF
     EVSINGRRYP QIGRVCMDQV VVSLGPVSEN PTESPVRPGD WAIIFGQDGP SVDEFAAAAG
     TIAYEILTLP RGPRVKRRFL QFDATTHPQP HNAAVTPAPA ALDLSQDSGS AVAPDADAMR
     DLGRQVGEQL LNQETAGGAA GTVVVLTGPL GAGKTTLTQG IAQGLGVRGR VQSPTFTIVR
     THKGTEGRPG MLHMDAYRLL GADVQEGIAP GEQMDRNVVL DALESLDLDA DLDSHVVVAE
     WGRGVVEFLS DSVLDVSIER AESEDSEERV VAWSWISRRP HEPAQDGK
//
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