GenomeNet

Database: UniProt
Entry: Q981H7
LinkDB: Q981H7
Original site: Q981H7 
ID   ALR3_RHILO              Reviewed;         388 AA.
AC   Q981H7;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JAN-2019, entry version 104.
DE   RecName: Full=Alanine racemase 3 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr3; OrderedLocusNames=mlr9371;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OG   Plasmid pMLa.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000013; BAB54978.1; -; Genomic_DNA.
DR   RefSeq; WP_010915793.1; NC_002679.1.
DR   ProteinModelPortal; Q981H7; -.
DR   SMR; Q981H7; -.
DR   EnsemblBacteria; BAB54978; BAB54978; BAB54978.
DR   KEGG; mlo:mlr9371; -.
DR   PATRIC; fig|266835.9.peg.7136; -.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; MLOT266835:G1G20-7226-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000552; Plasmid pMLa.
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; Plasmid; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    388       Alanine racemase 3.
FT                                /FTId=PRO_0000114553.
FT   ACT_SITE     41     41       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     304    304       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      41     41       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   388 AA;  41130 MW;  04355B8341D254A3 CRC64;
     MLTSVRPADV VLEIDLSAIQ ANFQTISALV GPQVRVAAVV KSDAYGLGLV KVAGALIDAG
     CDLLFVGNLH EALLLRSSHI SAAVAVFCDE FARYGEHYRS NGLIPVVNNS VELDAICGAR
     EPQAYFLNVE TGLSRLGLAF DDVRRRYLGG IFKRRPPSVV LSHLACSERA GDAMNLLQWN
     RFRATSDLLK PTLLSLAASA GVWLGKRYHF DMVRVGSALY GLNSAGIRPN PLKPVVGVKA
     KTLDARNVAR SEAVGYGATF RTGRASRLAI AGIGYKHGLP WACANKISVR FAGYSAPLVG
     RVSMEYITID VTDVPEALCG PGTNVELLSD DFTVDDLAAS AGVHPQEVLT RLGVGCARQY
     LDGSSASAGF PGNLTNAGPG HDPRAILG
//
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