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Database: UniProt/TrEMBL
Entry: E3H5M4_ROTDC
LinkDB: E3H5M4_ROTDC
Original site: E3H5M4_ROTDC 
ID   E3H5M4_ROTDC            Unreviewed;       437 AA.
AC   E3H5M4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   28-FEB-2018, entry version 55.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:ADP39714.1};
GN   OrderedLocusNames=HMPREF0733_10256 {ECO:0000313|EMBL:ADP39714.1};
OS   Rothia dentocariosa (strain ATCC 17931 / CDC X599 / XDIA).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX   NCBI_TaxID=762948 {ECO:0000313|EMBL:ADP39714.1, ECO:0000313|Proteomes:UP000000387};
RN   [1] {ECO:0000313|Proteomes:UP000000387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17931 / CDC X599 / XDIA
RC   {ECO:0000313|Proteomes:UP000000387};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G.,
RA   Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W.,
RA   Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J.,
RA   Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D.,
RA   Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A.,
RA   Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L.,
RA   Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R.,
RA   Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RT   "The complete genome of Rothia dentocariosa ATCC 17931.";
RL   Submitted (OCT-2010) 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; CP002280; ADP39714.1; -; Genomic_DNA.
DR   RefSeq; WP_013397592.1; NC_014643.1.
DR   ProteinModelPortal; E3H5M4; -.
DR   STRING; 762948.HMPREF0733_10256; -.
DR   EnsemblBacteria; ADP39714; ADP39714; HMPREF0733_10256.
DR   GeneID; 29743626; -.
DR   KEGG; rdn:HMPREF0733_10256; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; RDEN762948-HMP:G1GOA-242-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000387; 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:UP000000387};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADP39714.1};
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:UP000000387}.
FT   DOMAIN      267    407       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     50     50       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    288    288       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     147    147       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     345    345       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      50     50       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   437 AA;  46730 MW;  EB3E27B86A9A5F81 CRC64;
     MTVPTRPLYT PNLQPGEAER TAIIDLNALE HNTRVLKDMI GERKLIAVVK ADAYGHGAYP
     VARSVLEAGA DILGVVHVTE ALELRSEGIT APIIAWLHTP QTDFDEALEA DIILGASGWD
     LEAIAEAANR TKKRARVHLK VDTGLGRNGS TFEDWPALVA RALELEAAGL VRIEGIFSHL
     AVADEPERPE TARQITRLNE FVTVARSAGL TPELVHLANS PGTITGASPL YNTNEAVLAD
     AVRCGIALYG LSPLAGVSSK DLNLRPVMTL GTHVCNVKEV PAGQGVSYGL RYSTDKPTTL
     ALIPLGYADG VPRIAEGAPV RIYPRADAAN PVEPRTYRVV GRIAMDQLVV DLEEPGLADP
     ARGILGGSAV LFGSGDNPPV EEWAAAAQTI NYEIVTRISP RVIRIYRGGA WVEREVDGLH
     ALGSLFGLDD EQTPETV
//
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