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Database: UniProt/TrEMBL
Entry: A6LX29_CLOB8
LinkDB: A6LX29_CLOB8
Original site: A6LX29_CLOB8 
ID   A6LX29_CLOB8            Unreviewed;       376 AA.
AC   A6LX29;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   28-FEB-2018, entry version 89.
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=Cbei_2758 {ECO:0000313|EMBL:ABR34909.1};
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR34909.1, ECO:0000313|Proteomes:UP000000565};
RN   [1] {ECO:0000313|EMBL:ABR34909.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
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., Sims D., Brettin T., Bruce D., Tapia R., Brainard J.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L.,
RA   Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W.,
RA   Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H.,
RA   Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-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; CP000721; ABR34909.1; -; Genomic_DNA.
DR   RefSeq; WP_012058964.1; NC_009617.1.
DR   ProteinModelPortal; A6LX29; -.
DR   STRING; 290402.Cbei_2758; -.
DR   EnsemblBacteria; ABR34909; ABR34909; Cbei_2758.
DR   KEGG; cbe:Cbei_2758; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; ISHFACA; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; CBEI290402:G1G93-2875-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000565; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000565};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ABR34909.1};
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:UP000000565}.
FT   DOMAIN      245    373       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   COILED       10     30       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     38     38       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    266    266       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     314    314       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   376 AA;  42072 MW;  FF57A2905EDD422A CRC64;
     MGEYFRTYAK IDLEAILHNI NEAKKRIERN VKIMAIIKAD GYGHGAAELG DFLKSEVDYY
     GVATLEEALE LRKSGIELPI LILGYTSPSQ YIEVVKNNIT QTVYNTEMAK EMSKAGAICK
     KEAKVHIALD TGMTRIGFDA NEDGIAEVQE ILTFSNLVVE GLFTHFATAD EADKSYSKLQ
     ISKYDKFVAL LEERDINIPI KHMCNSAGIM EFDHHRFDMV RCGIITYGLY PSEEVNKNAI
     TLKPALQWKT HVINVNIVDA GHGVSYGKTY ITKNETKIAT LSVGYADGYP RALSSKGRVL
     IHGKYAPIIG RICMDQMMVD VTHIDNVKIE DEVTLVGKDG ENIIYVEELA NMAGSFNYEF
     VCGIGKRVQR LYRELA
//
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