GenomeNet

Database: UniProt
Entry: Q8RAK6
LinkDB: Q8RAK6
Original site: Q8RAK6 
ID   ALR1_CALS4              Reviewed;         388 AA.
AC   Q8RAK6;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   16-JAN-2019, entry version 107.
DE   RecName: Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr1; OrderedLocusNames=TTE1207;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 /
OS   JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J.,
RA   Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L.,
RA   Tan H., Chen R., Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AE008691; AAM24437.1; -; Genomic_DNA.
DR   RefSeq; WP_011025537.1; NC_003869.1.
DR   PDB; 4Y2W; X-ray; 2.70 A; A/B=1-388.
DR   PDBsum; 4Y2W; -.
DR   ProteinModelPortal; Q8RAK6; -.
DR   SMR; Q8RAK6; -.
DR   STRING; 273068.TTE1207; -.
DR   EnsemblBacteria; AAM24437; AAM24437; TTE1207.
DR   KEGG; tte:TTE1207; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; SGAAMYH; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; TTEN273068:G1FZJ-1298-MONOMER; -.
DR   BRENDA; 5.1.1.1; 6784.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000555; 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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Isomerase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    388       Alanine racemase 1.
FT                                /FTId=PRO_0000114588.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   STRAND        8     14       {ECO:0000244|PDB:4Y2W}.
FT   HELIX        15     28       {ECO:0000244|PDB:4Y2W}.
FT   STRAND       34     38       {ECO:0000244|PDB:4Y2W}.
FT   HELIX        40     45       {ECO:0000244|PDB:4Y2W}.
FT   HELIX        48     58       {ECO:0000244|PDB:4Y2W}.
FT   STRAND       61     67       {ECO:0000244|PDB:4Y2W}.
FT   HELIX        68     76       {ECO:0000244|PDB:4Y2W}.
FT   STRAND       83     85       {ECO:0000244|PDB:4Y2W}.
FT   HELIX        91     93       {ECO:0000244|PDB:4Y2W}.
FT   HELIX        94     99       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      103    106       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       109    121       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      126    132       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      134    136       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      138    142       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       144    155       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      160    166       {ECO:0000244|PDB:4Y2W}.
FT   TURN        172    175       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       177    195       {ECO:0000244|PDB:4Y2W}.
FT   TURN        196    198       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      202    208       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       209    214       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       216    219       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      220    224       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       227    230       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      236    238       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      248    253       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      256    260       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      265    267       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       268    270       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      278    284       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       287    289       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       293    295       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      300    303       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      306    312       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      319    322       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      334    340       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       348    354       {ECO:0000244|PDB:4Y2W}.
FT   HELIX       359    365       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      372    376       {ECO:0000244|PDB:4Y2W}.
FT   STRAND      379    384       {ECO:0000244|PDB:4Y2W}.
SQ   SEQUENCE   388 AA;  44126 MW;  8D8E10CF5E20DC9E CRC64;
     MKFDGVRPTR VEVYLDAITH NFREIKKIVG KNVKIMAVIK GDAYGHGASY VAKFLEKEGV
     DYFGVATTEE ALELREKGIK TPILIFGYTP PTQLRQIVKH DLTQTVYDIK YAKELEKESL
     KQNKRAKVHI KIDTGLGRIG YIDFDLAQKE ILEMANMRGL ILEGIYSHFA AASEDDRDYC
     KEQFDKFMNL ISSLEKKRLK IPLKHIANAA AILNLNYSHL DMVRPGIILF GAYPSKRVER
     KVELRETLRF TTRVVHLKDV PAGFFIGYGK SFVTKRKSVI ATIPVGYADG LDRRLSNNYK
     LLLKGKYVPI VGRVCMDQCM IDVTDVEGVE IGDEVVIIGT QNNETVSVES MADKIETIPQ
     EVFSRISRRV PRVYFYDGIK IGEVNYLK
//
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