GenomeNet

Database: UniProt
Entry: O67687
LinkDB: O67687
Original site: O67687 
ID   ALR_AQUAE               Reviewed;         338 AA.
AC   O67687;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JAN-2019, entry version 120.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=aq_1827;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07650.1; -; Genomic_DNA.
DR   PIR; E70457; E70457.
DR   RefSeq; NP_214253.1; NC_000918.1.
DR   RefSeq; WP_010881190.1; NC_000918.1.
DR   ProteinModelPortal; O67687; -.
DR   SMR; O67687; -.
DR   STRING; 224324.aq_1827; -.
DR   PRIDE; O67687; -.
DR   EnsemblBacteria; AAC07650; AAC07650; aq_1827.
DR   GeneID; 1193494; -.
DR   KEGG; aae:aq_1827; -.
DR   PATRIC; fig|224324.8.peg.1411; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   InParanoid; O67687; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; AAEO224324:G1G15-1305-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000798; 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; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    338       Alanine racemase.
FT                                /FTId=PRO_0000114495.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    236    236       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     126    126       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     284    284       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      33     33       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   338 AA;  38203 MW;  376A3E0327E80752 CRC64;
     MPRAILEINS ERIRHNVKKL SEFSGKKVIA VIKADAYGIG SIQMAKILEP IEEVDAFAVA
     CVEEGVELRK MGIKKEILIL GGVLKDEVPL VEEYFLTPVV SDIEHLRAIG NRDIKFHVKY
     DTGMGRLGFL NEVIHDPRVE GIMSHLSSPA DEEFSKLQIK KFEEIVKKYT KVEKIHMESS
     AGVVYRVPFT THIRVGLAMY GEKPLKNYPV DIKPALTLKA KLISVKELPE NYPVSYSRTY
     VTKKKTKTGV VAFGYADGLM KTLSNRSYLL YKGEKLPIFG NITMDMTIVD LKNTDAKVGD
     WVYVVNEERT FTELAREAGT IPYELMCNLS KRIKRVVV
//
DBGET integrated database retrieval system