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Database: UniProt/TrEMBL
Entry: A3DIW7_CLOTH
LinkDB: A3DIW7_CLOTH
Original site: A3DIW7_CLOTH 
ID   A3DIW7_CLOTH            Unreviewed;       391 AA.
AC   A3DIW7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-SEP-2017, entry version 87.
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=Cthe_2697 {ECO:0000313|EMBL:ABN53896.1};
OS   Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 /
OS   NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium
OS   thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN53896.1, ECO:0000313|Proteomes:UP000002145};
RN   [1] {ECO:0000313|Proteomes:UP000002145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536
RC   / VPI 7372 {ECO:0000313|Proteomes:UP000002145};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) 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; CP000568; ABN53896.1; -; Genomic_DNA.
DR   ProteinModelPortal; A3DIW7; -.
DR   STRING; 203119.Cthe_2697; -.
DR   EnsemblBacteria; ABN53896; ABN53896; Cthe_2697.
DR   KEGG; cth:Cthe_2697; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002145; 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   Complete proteome {ECO:0000313|Proteomes:UP000002145};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ABN53896.1};
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:UP000002145}.
FT   DOMAIN      249    378       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     41     41       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     139    139       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      41     41       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   391 AA;  43669 MW;  E8D3E5C6DD62681E CRC64;
     MGMDYKFNRA WAEVNLDNIA HNVKEIRRIV DKKVEIMGVV KADAYGHGVM EIARTLLENG
     VTRLAVSMLD EAIQLRQNGI KVPILILSYT DPVRAEEIVL NDVTQTVFSH DLAEALSEAA
     VKHHRNVKIH IKIDTGMTRV GFMPGYSAVK NVVQISKLPG IIIEGLFTHF ASADEADKSY
     TYMQFERFMS IVGELNRIGV YIPVKHVCNS AALIEFPEMH LNMVRPGIAL YGLYPSDEVD
     KTKIDLRPAM SLKANVILVK DVEKDTFISY GRIFKTSRNS RIATIPIGYA DGYTRLLTGK
     GKVLLNGQLA PIVGRICMDQ CMVDITDIEG DVKVGDEAVL IGKQKDNEIK VEDLAKSVGT
     INYELVSIIG KRIPRVYLKE GKIYNVLNYL I
//
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