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Database: UniProt/TrEMBL
Entry: F6CKT7_DESK7
LinkDB: F6CKT7_DESK7
Original site: F6CKT7_DESK7 
ID   F6CKT7_DESK7            Unreviewed;       379 AA.
AC   F6CKT7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   28-FEB-2018, entry version 50.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=Desku_1293 {ECO:0000313|EMBL:AEG14876.1};
OS   Desulfotomaculum kuznetsovii (strain DSM 6115 / VKM B-1805 / 17).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=760568 {ECO:0000313|EMBL:AEG14876.1, ECO:0000313|Proteomes:UP000009229};
RN   [1] {ECO:0000313|EMBL:AEG14876.1, ECO:0000313|Proteomes:UP000009229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6115 / VKM B-1805 / 17 {ECO:0000313|Proteomes:UP000009229};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Saunders E., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Nazina T.,
RA   Ivanova A., Parshina S., Kuever J., Muyzer G., Plugge C., Stams A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfotomaculum kuznetsovii DSM 6115.";
RL   Submitted (MAY-2011) 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, ECO:0000256|SAAS:SAAS00630646}.
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, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP002770; AEG14876.1; -; Genomic_DNA.
DR   ProteinModelPortal; F6CKT7; -.
DR   STRING; 760568.Desku_1293; -.
DR   EnsemblBacteria; AEG14876; AEG14876; Desku_1293.
DR   KEGG; dku:Desku_1293; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; ISHFACA; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; DKUZ760568:GHV4-1259-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000009229; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000009229};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AEG14876.1};
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:UP000009229}.
FT   DOMAIN      249    377       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     43     43       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    270    270       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     318    318       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      43     43       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   379 AA;  40992 MW;  DB23E04E25293590 CRC64;
     MITESCSNGR PVWVEVNLGA VARNVREIRK LLQPGTKLMA VVKADAYGHG ALPVARAALA
     NGAECLAVAI LDEALALRRG GITAPILILG YTPPEQASFL VEYDLTQTVF SLDAVQAISA
     AAAAAGKTAR VHIKVDTGMG RIGVFPSEAP DFAEAVSRLP NIFIEGVYTH MACADEQDKA
     YTRWQFDRFK EAVAGIEARG VAIPLKHVAN SATTLDLPEM HLDMVRTGII LYGLWPSPDV
     RRVIDLKPAM QLKTRVAYVK QVPAGTSISY GRTFTTTGPS VIATLPLGYA DGWSRLLSNK
     AEVLIHGQRA PLVGRVCMDQ CMVDVTRIPG VRPGDEVVLF GVQGEQFLPV EEVASHMGTI
     NYEMVCLISK RVPRIYLND
//
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